Lipid-and-Metabolism reagents: Novus Biologicals

NB300-221

GAPDH Antibody (1D4) - BSA Free

(19 Reviews)

(455 Publications)

0.1 ml

NB300-221

Analysis of GAPDH in human nucleus pulposus cell culture (40ug/lane) using anti-GAPDH antibody. LI-COR Odyssey imaging system was used for detection. Western blot image submitted by a verified customer review.

Analysis of of HeLa cells stained with GAPDH antibody, dilution 1:100 (Green). DAPI staining of nuclear DNA (Blue). The GAPDH antibody produces strong cytoplasmic staining of healthy cells.

Analysis of cell line lysates probed with mouse mAb to GAPDH (theoretical molecular weight: 36 kDa), NB300-221, dilution 1:2,000: [1] protein standard, [2] HEK293, [3] HeLa, [4] SH-SY5Y, [5] COS1, [6] NIH-3T3, and [7] C6 cells. The GAPDH antibody reveals a single band at ~37 kDa in all cell lines. GAPDH is a house keeping protein, the level of which is relatively unaffected by most experimental manipulations, and, as a result, this antibody has been widely used as a western blotting loading control.

Human eye cell lysate. Antibody used at 1:500. WB image submitted by a verified customer review.

Analysis of GAPDH in chicken pectoralis major using anti-GAPDH antibody. The primary antibody was used at a dilution of 1:4000, incubated for 1 hour at room temperature. Western blot image submitted by a verified customer review.

Application of the approach to other cell lines. The remainder of the protocol from Figure 2 was then applied using 100 ug/mL digitonin as the optimal cytosolic extract in each case. An aliquot of each extract was then analyzed by 4-12% SDS PAGE followed by Western blotting and probing with antibodies to GAPDH, BiP and Histone H3 (Used as an alternative nuclear marker due to weakness of the Lamin A signal in HeLa cells). Image collected and cropped by CiteAb from the following publication (//bmcresnotes.biomedcentral.com/articles/10.1186/1756-0500-2-243) licensed under a CC-BY license.

Endothelial responses provoked by Hb-lipid interactions are attenuated by sulfide donors. Confluence HAoECs were exposed to the obtained Hb samples for 8 hours and VCAM-1 expression was determined by Western blotting. GAPDH were used as a loading control. Representative experiment, n = 3. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/omcl/2018/3812568/), licensed under a CC-BY license.

Regulation of cell migration-associated proteins by NCKU-21 in A549 and CL1-5 cells. Protein expressions of matrix metalloproteinase-2 (MMP-2) and MMP-9 were analyzed in A549 cell treated with NCKU-21 for 24 hr. * P 1.2 to ≤1.3) & high (>1.3) of 3 × MYC-GFP-Bub1 signal & localization in live cells synchronized in mitosis by a thymidine release. Data represent the mean±s.e. of 3 independent experiments, with 58–61 cells measured per condition. Significance was measured for the high group by one-way analysis of variance (ANOVA) & pairwise t-test (Holm–Sidak). (e) Scatter plot of the cytoplasm versus kinetochore GFP levels of individual cells from each of the stable cell lines. The number of cells, R2 (measure of the goodness-of-fit) & significance (one-way ANOVA) are indicated. (f) Western blottings showing levels of the 3 × MYC-GFP-Bub1 proteins in the stable cell lines in whole cell extracts (left) & in cytoplasmic extracts (right). Scale bar, 10 μM. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/ncomms9364), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: GAPDH Antibody (1D4) [NB300-221] - Notch1, ApoER2 & Dab1 colocalize in hippocampal neurons. (A) Representative image of fluorescent immunolabeling shows that Notch1 is localized in a subset of CA3 neurons, co-expressing Dab1 & ApoER2 (magnified insert). ApoER2 is highly expressed in all CA3 neurons. (B) Fluorescent immunolabeling shows the distribution of Notch1 & Dab1 as compared to Arc/Arg3.1 in CA3 neurons. (B′) Close up of a dendrite showing colocalization of the three proteins (white arrowheads). (C) Western blot analysis on immunoprecipitated samples from whole hippocampal lysate shows that Notch1 displays a strong interaction with Dab1 whereas Notch1 & ApoER2 interaction appears weaker in the preparation (n = 4 independent experiments). (D) Immunolabeling on immunoprecipitated samples from whole cortical lysates show that Notch1 & Dab1 interact. ApoER2 is bound to both Notch1 & Dab1 (n = 3 independent experiments). (E) Co-IP from synaptosomal membrane fractions reveals a stronger interaction between Notch1 & ApoER2, which is reduced in the N1cKO (n = 3 independent pulldowns). In (C–E) GAPDH is used as a loading control for the inputs & to detect contamination in the IP samples. Scale bar in (A) is 50 μm & (B) 25 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26635527), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Reduced expression of UNC5A in FancC−/− cells. a Reduced expression of Unc5A in brain cortex of FancC−/− mice compared to wild-type littermates. Western blotting was performed with the indicated antibodies. Each lane represents a different animal (WT: n = 6; FancC−/−: n = 8). b Bar graph represents ratio of Unc5A normalized to tubulin from WT (n = 6) & FancC−/− mice (n = 8). c Bar graph representation of UNC5A expression normalized to Sdha & Tbp from wild-type (WT) & FancC−/−-derived fibroblasts (n = 3). RLU: Relative light units. d–f HEK293T cells were transfected with UNC5AICD, FANCE & FANCC constructs expressing full-length FANCC (in d), FANCC1–306 (in e) or FANCC307–558 (in f). Constructs were transfected at a molecular ratio of 1:1:1 or with 10 times the molar amount of FANCE, FANCC or UNC5AICD as indicated in the figure. The total amount of transfected plasmid was equalized for all strategies with control empty vectors. Representative immunoblots performed with anti-HA (UNC5AICD), anti-FANCC, anti-FANCE or anti-GAPDH antibodies are shown. Arrows indicate appropriate protein bands. Bar graphs represent the mean fold change ± SEM of UNC5A protein levels normalized to GAPDH compared to 1:1:1 transfection controls in at least 4 separate experiments. *p < 0.05; **p < 0.005 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30213274), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Depletion of RAD21 & other cohesin subunits leads to differentiation of ESCs.(A): qPCR analysis of esiRNA knock-down efficiency for indicated genes (48 h RNAi, n = 3, error bars denote s.d. & *, ** indicate p<0.05 & 0.01 respectively). Transfection of a non-targeting esiRNA (Luc) was used as a control. Numbers adjacent to the gene names indicate independent, non-overlapping esiRNAs transfected. (B): Western Blot analysis of esiRNA knock-down efficiency for indicated genes (48 h RNAi; esi-1 & esi-2 indicate independent, non-overlapping esiRNAs transfected). Transfection of a non-targeting esiRNA (Luc) was used as a control. GAPDH served as a protein loading control. (C): Alkaline phosphatase staining of ESCs, which had been transfected with esiRNAs targeting RAD21, SMC1a & SMC3 (72 h post RNAi) showed a strong differentiation phenotype compared to a control (Luc). Nanog depletion served as a positive control for ESC differentiation. Scale bars correspond to 100 µm. (D): Quantification of alkaline phosphatase staining (n = 3) separated into undifferentiated (green), mixed (yellow) & differentiated colonies (red). (E+F): qPCR validation of expression changes of (E) stem cell maintenance genes & (F) lineage marker genes upon knock-down of RAD21 (two independent esiRNAs) & Luc control (48 h RNAi, n = 3, error bars denote s.d. & *, **, *** indicate p<0.05, 0.01 & 0.001 respectively). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/21589869), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Application of the approach to other cell lines. (A) HT1080 cells (2 × 105) & HeLa cells (1 × 105) were plated in the wells of a 12 well plate & the digitonin concentration required for optimal extraction of the cytosol was determined as in Figure1. (B) The remainder of the protocol from Figure 2 was then applied using 100 μg/ml digitonin as the optimal cytosolic extract in each case. An aliquot of each extract was then analyzed by 4-12% SDS PAGE followed by Western blotting & probing with antibodies to GAPDH, BiP & Histone H3 (Used as an alternative nuclear marker due to weakness of the Lamin A signal in HeLa cells). (C) Samples were analyzed by 4-12% SDS PAGE followed by staining with Coomassie blue & then silver staining showing the difference in protein composition of each sample. The bracket alongside the gels marks the position of Histones in the RIPA nuclear extract & the asterisk next to the silver stained gels denotes protein bands unique to the E-RIPA extracts. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/20003239), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: GAPDH Antibody (1D4) [NB300-221] - Role of the TRIM11-USP14 axis in cell growth & apoptosis. a Levels of endogenous TRIM11 in HCT116 cells grown at 43 °C for 0 or 90 min, or at 43 °C for 90 min, & then at 37 °C for 60 or 120 min. b, c Levels of endogenous TRIM11 (b), or Flag-TRIM11, the indicated proteasome subunits, & USP14 (c) in the SN & P fractions of HCT116 cells with & without heat shock at 43 °C for 90 min. d, g TRIM11 overexpression (d) or knockdown (g) HCT116 cells & the corresponding control cells grown under unstressed, heat shock, & heat shock plus recovery conditions were analyzed for K48 polyUb conjugates & caspase-3 activation. e, f, h Apoptosis in TRIM11 overexpression (e, f) or knockdown (h) HCT116 cells, & the corresponding control HCT116 cells, treated with & without heat shock. i, j Caspase-3 activation (i) & apoptosis (j) in HCT116 cells expressing the indicated proteins and grown under normal or heat stress conditions. k–m K48 polyUb conjugates, caspase-3 activation (k), amyloid-like fibrils (l), & apoptosis (m) in HCT116 cells expressing the indicated proteins and grown under normal & heat stress conditions. In e, f, h, j, l, & m, data represent mean ± SEM (n = 3 unless otherwise indicated). *P < 0.05; **P < 0.01; ***P < 0.001. Uncropped blots are presented in Supplementary Fig. 14 Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-018-03499-z), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Reactivity:

Hu, Mu, Rt, Po, Av, Bv, Ca, Ch, ChHa, Dr, Eq, Fe, Ha, Ma-Op, Pm, Rb, Sh, Ze

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Av, Bv, Ca, Ch, ChHa, Dr, Eq, Fe, Ha, Ma-Op, Pm, Rb, Sh, Ze

Applications:

, , , , , , ,

Applications: , , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Formulations

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BSA Free	NB300-221SS

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BC100-494

PINK1 Antibody - BSA Free

(13 Reviews)

(300 Publications)

0.1 ml

BC100-494

$PINK1/Parkin-mediated mitophagy. Western Blot of mitochondrial and cytosolic fractions for PINK1, Parkin, and ubiquitin. E Quantitation of protein levels, normalized to VDAC and GAPDH, Ubiquitin: n = 6, PINK1: n = 5, Parkin: n = 8. R, post-reoxygenation. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33980811/) licensed under a CC-BY license.$

Confocal microscopy analysis of the mitophagy initiation in the RPE cells by staining PINK1 and PARKIN. One-year-old WT and dKO mice focusing on the RPE cells in the vicinity of the optic nerve (a,e). PINK1 (b, red) and PARKIN (c, green) were double-stained and the merged image (d) was used to count the colocalized puncta from WT. Similarly, in dKO PINK1 (f, red) and PARKIN (g, green) were double-stained, and the merged image (h) was used to count the colocalized puncta. dKO = NFE2L2/PGC1a double knockout. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32183173/) licensed under a CC-BY license.

Western blot image of PINK1 antibody (BC100-494) in multiple cells lines. Human HeLa (lane 1), Mouse NIH-3T3 (lane 2), L929 (lane 3) and Rat PC12 (lane 4) whole cell protein were separated by SDS-PAGE on a 7.5% polyacrylamide gel. Protein was transferred to PVDF membrane and probed with 2 ug/mL BC100-494 in 1% BSA and detected with an HRP-conjugated anti-rabbit secondary antibody using chemiluminescence. Observed molecular weight ~55 kDa (arrowhead).

Analysis of PINK1 in mouse liver and hypatocytes using PINK1 antibody. Observed molecular weight ~55 kDa. WB image submitted by a verified customer review.

Pathogenic mutants of Parkin are subjected to Ser65 phosphorylation. Phos-tag Western blotting for Parkin and Western blotting for PINK1 were performed using Parkin WT and a series of pathogenic mutants. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep01002) licensed under a CC-BY license.

Alteration of mitochondria and PD associated proteins in SH-SY5Y cells with telomere removal by CRISPR-Cas9. Representative Western blot of PGC-1alpha, NRF1, and PINK1 in SH-SY5Y cells transfected with either gTel or gCont (72 h). Beta-actin served as a loading control. Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/1422-0067/18/10/2093), licensed under a CC-BY license.

35 ug Neuro2A whole cell lysate separated on 8% PAGE and stained for PINK1 (1:1000 in 5% milk powder in TBST; secondary antibody AP at 1:5000). WB image submitted by a verified customer review.

Rabbit heart tissue. IHC-P image submitted by a verified customer review.

HEK293 cells were co-transfected with PINK1 siRNA (#1 or #2) or scrambled siRNA (scrambled) and untagged wild-type (WT) or Ser65Ala (S65A) mutant Parkin as indicated using TransFectin reagent (Bio-Rad). 48 hrs post-transfection, cells were treated with/without 10 uM CCCP for 3 h. 0.25 mg of 1% Triton whole-cell lysate were subjected to immunoprecipitation with GST-Parkin antibody (S966C) covalently coupled to protein G Sepharose and then immunoblotted with anti-phospho-Ser65 antibody in the presence of dephosphorylated peptide. 5% of the IP was immunoblotted with total anti-Parkin antibody. 0.25 mg of whole-cell lysates were immunoprecipitated with anti-PINK1 antibody (S085D) and immunoblotted with anti-PINK1 antibody. Representative of three independent experiments. Image collected and cropped by CiteAb from the following publication (//rsob.royalsocietypublishing.org/cgi/doi/10.1098/rsob.120080) licensed under a CC-BY license.

Characterisation of mitochondrial content and function in PINK1-/- platelets. Cropped immunoblots showing PINK1 expression in 10 uM CCCP (6 hours) treated WT, but not KO platelets by IP (upper panel) with loading control of IP inputs by blotting for PINK1 (lower panel). Uncropped blots for PINK1 are provided in Supplementary Fig. S1b. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-018-32716-4), licensed under a CC-BY license.

Representative TEM picture. The red and green arrows indicate PINK and PARKIN immunogold particles in the dKO RPE samples, respectively (e). ML, melanosome. Scale = 0.2 um. Mitochondria (M). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32183173) licensed under a CC-BY license.

Protein content and oxidation. Gastrocnemius muscle was analyzed by immunoblotting (A) for oxidatively modified protein, STIM1, PARKIN, PINK1, PGC‐1 alpha , VDAC1, and 4HNE (B). Data are means ± SEM. *Significantly different from Tp53inp1+/+.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - PPM1H does not dephosphorylate Ser111 of Rab8A or key phosphorylation sites of AMPK & Akt signaling pathways.(A) HEK293 cells were transiently transfected with constructs expressing the indicated components. 24 hr post-transfection, cells were treated ±10 µM CCCP (Carbonyl cyanide m-chlorophenyl hydrazine) for 3 hr to induce activation of the PINK1 kinase & trigger Rab8A phosphorylation at Ser111 (Lai et al., 2015). (B) As in (A) except cells were immunoblotted with the indicated antibodies that recognize key phosphorylation sites of AMPK & Akt signaling pathways. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31663853), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - PINK1 & Parkin are phosphorylated after a decrease in delta Ψm in mouse primary neurons. Neurons were infected with lentivirus encoding PINK1-Flag (A), wild-type HA-Parkin (B) or HA-Parkin with either the S65A or S65E mutation (C). Cells were treated with the mitochondrial uncoupler CCCP (30 μm) for 1–3 h & subjected to SDS-PAGE in the absence or presence of 50 μm phos-tag. Note that mobility does not reflect the molecular weight of proteins in phos-tag PAGE (Kinoshita et al. 15), & thus, molecular weight markers are not shown in the bottom gels. The red & black asterisks in (C) indicate phosphorylation of Parkin at Ser65 & an additional minor phosphorylation site, respectively. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23751051), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - PINK1 translation is critical for the accumulation of PINK1 upon mitochondrial damage. aPINK1 mRNA levels were not altered by mitochondrial damage. HeLa cells were incubated with 10 μM CCCP or combination of 10 μM oligomycin & 4 μM antimycin for 2 h & then, PINK1 mRNA levels were measured by qRT-PCR. PINK1 mRNA level was normalized to the corresponding GAPDH levels & quantified as a percentage of control (n = 8, t-test). b, c Translation is involved in PINK1 accumulation upon CCCP treatment. HeLa cells were first pre-incubated with 100 μM cycloheximide (CHX) for 2 h & then washed. Cells were further incubated with 10 μM CCCP with or without CHX for 2 h (n = 4, two-way ANOVA). Values are mean ± SEM (n.s. = non-significant, ***p 1000 cells) & are shown as a percentage of control. Values are mean ± SEM (*p < 0.05, **p < 0.01, ***p < 0.001) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27456084), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Inhibition of endogenous miR-27a/b function increases human PINK1 expression. a Schematic diagram of sequence alignment of miR-27a/b & anti-miR-27a/b. Asterisks (*) indicate conserved nucleotides. b Inhibition of endogenous miR-27a/b function increased luciferase activities in HeLa cells. Cells were transfected with the reporter constructs containing the full-length 3′UTR of human PINK1 mRNA with wild-type (WT) or mutated (Mut) seed match sites downstream of Renilla luciferase gene. 48 h post-transfection, luciferase activities were measured (n = 4, t-test). c-f Inhibition of endogenous miR-27a/b increased PINK1 protein levels in HeLa (C-D) & M17 cells (E-F). Cells were transfected with 150 nM of anti-miR-27a/b or anti-control (anti-Ctl). 48 h post-transfection, cells were harvested for Western blot. PINK1 protein level was normalized to corresponding GAPDH level & quantified as a percentage of control (n = 4, t-test). Data are shown as a percentage of control. Values are mean ± SEM (n.s. = non-significant, **p < 0.01, ***p < 0.00) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27456084), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Regulation of PINK1 by miRNA. a Schematic diagram of AGO-specific RNA immunoprecipitation assay. b, cPINK1 mRNAs are associated with miRNA/RISC complex. HeLa cells were transfected with 50 nM of AGO2 siRNA or negative control. 48 h post-transfection, AGO2-bound mRNAs were pulled down from cell lysates with 2A8 anti-AGO2 antibody or non-specific IgG antibody. PINK1 mRNA levels were then measured by qRT-PCR. siRNA against AGO2 served as a quality control for AGO-specific RNA immunoprecipitation assay. PINK1 mRNA levels were quantified as a percentage of group 1 (n = 6, two-way ANOVA). d, e Knock-down of DICER1 increased PINK1 protein levels. HeLa cells were transfected with 50 nM DICER1 siRNA (DICER1 KD) or negative control (Ctl). 48 h post-transfection, cells were harvested for Western blot. The arrowhead indicates a full-length PINK1 band & the asterisk indicates a non-specific band. Each protein level was normalized to corresponding GAPDH level & quantified as a percentage of control (n = 4, t-test). Values are mean ± SEM (n.s. = non-significant, **p < 0.01, ***p < 0.001) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27456084), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - The expression levels of microtubule protein light chain 3 (LC3B), PTEN inducing putative kinase 1 (PINK1), Parkin, mitofusin 1 (Mfn1), toll-like receptor (TLR) 9, cytochrome c oxidase 4 (COX4), myeloid differentiation factor 88 (MyD88), & nuclear factor (NF)-kappa B in lung tissues from animals with spontaneous breathing (CON) or mechanical ventilation at high tidal volume (HTV) with saline, antimycin A (AmA) or cyclosporine A (CsA). (A) Levels of PINK1, Parkin, & Mfn1 mRNA. (B) Levels of LC3B, PINK1, Parkin, & Mfn1 protein by Western blot. (C) Relative expression of LC3B-II/LC3B-I & PINK1 protein. (D) Relative expression of Parkin & Mfn1 protein. (E) Levels of TLR9 & COX4 mRNA. (F) Levels of MyD88 & nuclear factor-kappa B (NF-kappa B) mRNA. (G) Levels of TLR9, COX4, MyD88, & NF-kappa B protein by Western blot. (H) Relative expression of TLR9 & COX4 protein. (I) Relative expression of MyD88 & NF-kappa B protein. Fold expression for target genes was normalized to that measured for the beta -actin gene. Both of these experiments were in triplicate. aP < 0.05 vs. CON group;bP < 0.05 vs. HTV group; & cP < 0.05 vs. AmA group. Image collected & cropped by CiteAb from the following publication (//www.frontiersin.org/article/10.3389/fimmu.2018.01477/full), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Mitophagy contributes to removal of excess mitochondrial fragments in preeclampsia.(a, left panel) Representative TEM image of a cytotrophoblast from PTC & PE placenta collected at 29 weeks. Mitochondrial proximity to ER (MAM) is indicated by white arrows, mitochondrial fission events are depicted by white stars (scale bar: 500 nm; n = 8 separate PE placentae). (a, right panel) percentage of mitochondrial tethering to the ER in in PE vs. PTC (PE placentae, n = 8; PTC placentae, n = 7; unpaired Student’s t-test *P < 0.05). b Representative western blots for MFN2 & calreticulin in ER isolated from PE & PTC placentae (PE & PTC, n = 3 separate samples). c WB & associated densitometry of ASAH2 (normalized to TOM20) in mitochondria from PTC & PE placentae. d Representative TEM depicting mitophagy (white arrow) in cytotrophoblast cell from PE placenta (scale bar: 500 nm, n = 8 separate PE placentae). e Western blot & associated densitometry of PINK1 & Parkin in PE vs. PTC mitochondrial isolates. Densitometry for PINK1 blot was used to calculate the ratio of full-length PINK63kDa to cleaved PINK153kDa (PE & PTC, n = 4 separate placentae, *P < 0.05) Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41419-018-0360-0), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Deficiency or mutant PINK1 reduces phosphorylation of LETM1 at Thr192. a, b Proteins extracted from PINK1 WT or KO MEFs (a) or mouse brain (b) were subjected to IP with anti-LETM1, probed with pT192 & reprobed with anti-LETM1 by WB. c Proteins extracted from human fibroblast of control (Con) or a PINK1-Q456X patient (Q456X) were subjected to IP with anti-LETM1, probed with pT192 & reprobed with anti-LETM1 by WB. d HEK293 cells were transfected with Adtrack GFP control, AdPINK1-WT, & AdPINK1-Q456X mutant for 1 day. Endogenous LETM1 protein was isolated by IP with anti-LETM1, probed with pT192 & reprobed with anti-LETM1 by WB. e SH-SY5Y cells were treated with 25 µM rotenone for 8 or 16 h. Total cell lysates were either analyzed by WB with anti-PINK1, or subjected to IP with anti-LETM1, probed with pT192 & reprobed with anti-LETM1 antibodies by WB. All above experiments were replicated three times, respectively Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29123128), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Polyphyllin I suppressed, & PINK1 knockdown further suppressed, tumor growth in a MDA-MB-231 xenograft modelA. Tumor volumes were measured every week & differed at the end of the treatment period (*P < 0.01 compared to shCon cells treated with PPI, ##P< 0.01 compared to shPINK1 cells treated with PPI). B. Representative image of tumors from each group. C. Body weight changes in mice during the 6 weeks of PPI treatment. There were no differences in body weights between the PPI-treated shCon & vehicle-treated shCon groups or between the PPI-treated shPINK1 group & shCon groups. D. Representative tumor tissues were sectioned & subjected to H&E staining, TUNEL assay, & immunohistochemistry staining for C-CASP3. Scale bars: 50 μm. E. Representative tumor tissues from each group were prepared & subjected to western blot using anti-DRP1, -PARK2, -LC3B, -PINK1, & -C-CASP3 antibodies. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.14413), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Corticosterone affects NIX-dependent mitophagy through decreasing PGC1 alpha in vivo.a–f Mice exposed to vehicle, corticosterone (10 mg/kg), corticosterone w/ phorbol 12-myristate 13-acetate (PMA pretreatment, 200 μg/kg), or PMA alone for 7 days. a Slide samples for IHC immunostained w/ LAMP1 (green), TOMM20 (red), & DAPI (blue). Scale bars, 100 μm (magnification, ×200). n = 5. b The expressions of NIX, PTEN-induced kinase 1 (PINK1), & BCL2 interacting protein 3 (BNIP3) detected w/ WB where beta -actin used as a loading control. n = 5. c Slide samples for IHC immunostained w/ synpatophysin (green), PSD95 (red), & DAPI (blue). Scale bars, 100 μm (magnification, ×200). n = 5. d Synaptophysin & PSD95 detected by WB. Loading control is beta -actin. n = 5. e The mice subjected to Y-maze test to evaluate spatial memory function. n = 6. f The mice subjected to forced swim test to evaluate depression-like behavior. n = 5. g Vehicle or RU 486 (5 mg/kg) injected mice presented w//w/out corticosterone (10 mg/kg) for 3 days. The expressions of peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC1 alpha ) & NIX visualized via WB. Loading control is beta -actin. n = 5. h The schematic model for mechanisms of inhibition in NIX-dependent mitophagy by glucocorticoid shown. All blots & IF images representative. n = 5 or 6 from each animal w/ two technical replicates each in results of IHC & WB. Quantitative data presented as a mean ± S.E.M. The representative images acquired by SRRF imaging system. Two-sided two-way ANOVA conducted except Fig. 8b, data of which analyzed by two-sided unpaired student’s t test. ** indicates p < 0.01 versus control & ## indicates p < 0.01 versus corticosterone, respectively. Data provided as a Source data file. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33473105), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Polyphyllin I triggers PINK1/PARK2-dependent mitophagyA. MDA-MB-231 cells were treated with 8 μM PPI for different periods of time as indicated, & PARK2, P62, & ubiquitin (UB) levels in mitochondrial fractions were determined by western blot. B. Cells were cotransfected with GFP-UB & RFP-mito & treated with 8 μM PPI for 9 h, after which PARK2 (Alexa Fluor 405, pink) & P62 (Alexa Fluor 647, blue) immunostaining was detected using confocal microscopy. C. Cells cotransfected with GFP-UB & RFP-LC3 were treated with 8 μM PPI for 9 h, after which PARK2 (Alexa Fluor 405, pink) & TOMM20 (Alexa Fluor 647, blue) immunostaining was detected using confocal microscopy. Scale bars: 10 μm. D-E. MDA-MB-231 cells were treated with 8 μM PPI for different periods of time as indicated; whole-cell lysates were then separated on 8% SDS-PAGE gels & analyzed by western blot using the anti-PINK1 antibody. Relative full-length (∼63 kDa) & cleaved (∼52 kDa) PINK1 levels were quantified by densitometry & normalized to Tubulin. The results were expressed as a percentage of control, which was set at 100%. Data are presented as mean ± SD (*P< 0.01 vs. the control). F. Cells were treated with 8 μM PPI for different periods of time as indicated, & whole-cell lysates were then subjected to western blot analysis. G. Cells were treated with 8 μM PPI for 9 h, after which mitochondrial fractions were prepared & subjected to immunoprecipitation using anti-PINK1 antibody; associated PARK2 was detected using immunoblotting. H. RFP-mito-expressing MDA-MB-231 cells were treated with 8 μM PPI for 9 h, & PINK1 (Alexa Fluor 488, green) & PARK2 (Alexa Fluor 405, pink) immunostaining were evaluated using confocal microscopy. Scale bars: 10 μm. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.14413), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - miR-27a/b suppress human PINK1 expression. a Schematic diagram of the conserved target sites of miR-27a/b in the 3′UTR of human PINK1 mRNA. Seed sequences were indicated in red. Asterisks (*) indicate the conserved nucleotides. b Schematic diagram of the luciferase reporter plasmids. The reporter constructs contain the full-length 3′UTR of human PINK1 mRNA with wild-type (WT) or mutated (Mut) seed match sites downstream of Renilla luciferase gene. c Overexpression of miR-27a/b decreased luciferase activities in HeLa cells. Cells were transfected with miR-27a/b or negative control (Ctl) along with reporter constructs as indicated. 48 h post-transfection, luciferase activities were measured (n = 4, one-way ANOVA). Renilla luciferase activity was normalized to the corresponding firefly luciferase activity. d-g Overexpression of miR-27a/b decreased PINK1 protein levels in HeLa (D-E) & M17 cells (F-G). Cells were transfected with miR-27a/b or negative control (Ctl). 48 h post-transfection, cells were harvested for Western blot (n = 4, t-test). PINK1 protein level was normalized to corresponding GAPDH level & quantified as a percentage of control. Data are shown as a percentage of control. Values are mean ± SEM (n.s. = non-significant, **p < 0.01, ***p < 0.001) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27456084), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Increased p62 expression is prevented in PINK1 knock‐down cells. (a) SH‐SY5Y cells expressing scrambled shRNA or PINK1 shRNA (117‐2, 118‐3, & 118‐4) were treated with 10 μM carbonyl cyanide m‐chlorophenylhydrazone (CCCP) for 24 h & full‐length (FL) PINK1 protein levels measured by western blot. No accumulation of FL PINK1 was observed in 118‐3 & 118‐4 PINK1 shRNA clones. (b) SH‐SY5Y cells constitutively expressing scrambled (scram) or PINK1 shRNA (clone 118‐3) were treated with vehicle or 10 μM CCCP for 24 h & p62 protein expression measured by western blotting. **p < 0.05 versus scram CCCP; n = 9. (c) SH‐SY5Y cells were incubated in serum‐free culture media for up to 24 h to induce starvation‐mediated macroautophagy. p62 protein levels were measured by western blotting. *p < 0.05 versus 0 h; **p < 0.01 versus 0 h; n = 4. (d) SH‐SY5Y cells were transfected with scrambled (scram) or p62 siRNA for 72 h. For the last 24 h, cells were treated with vehicle (ethanol) or 10 μM CCCP. p62 protein expression was then measured by western blotting. p62 protein was significantly decreased in p62 siRNA cells under basal conditions & following CCCP treatment, when compared to scram cells. **p < 0.01 versus scram vehicle or scram CCCP; n = 3. (e) Mitochondrial content was measured in SH‐SY5Y cells treated with scram or p62 siRNA for 72 h by measuring citrate synthase (CS) activity. For the last 24 h, cells were treated with vehicle or 10 μM CCCP & data are expressed as % of vehicle. *p < 0.05 versus scram CCCP treatment; n = 5. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26509433), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - NF kappa B upregulates human PINK1 gene expression. (A) NF kappa B increases the endogenous human PINK1 mRNA level. HEK293 cells were transfected with either the NF kappa B expression vector or empty vector pMTF. RT-PCRs were performed using either primers specific to the human PINK1 coding sequence or the human beta -actin coding sequence. (B) NF kappa B increases the endogenous human PINK1 protein levels. HEK293 cells transfected with NF kappa B were harvested 48 h after transfection for protein detection. Cell lysates were run on 10% glycine gel & images were collected by Licor. A significant increase of endogenous PINK1 was observed. (C) The endogenous human PINK1 protein level was dramatically increased by NF kappa B in SH-SY5Y cells. SH-SY5Y cells were transfected with NF kappa B p65 plasmids or the control vector pMTF & then harvested for protein detections. The human PINK1 protein & its proteolysis products ∆1-PINK1 (55kD) & ∆2-PINK1 (45kD) were all increased. beta -actin acted as the internal control. (D) LPS treatment facilitated PINK1 expression in SH-SY5Y cells. Cells were harvested after being treated for 16 h & then subjected to Western blot. The human beta -actin level was served as a control. Quantification was performed by Image J software. Values indicate means ± SEM. n = 3, *p <0.01 by Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25108683), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - G-TPP induces PINK1 stabilization & kinase activity in HeLa cells(A) G-TPP treatment leads to PINK1 stabilization & pS65-Ub induction in HeLa cells. HeLa cells stably expressing untagged Parkin were treated with 10 µM G-TPP for the indicated times. Western blots were prepared with cell lysates & probed with antibodies against PINK1 & pS65-Ub. GAPDH served as a loading control. (B) pS65-Ub is induced in G-TPP treated cells & co-localizes with EGFP-Parkin & mitochondria. HeLa cells stably expressing EGFP-Parkin (green) were treated with 10 µM G-TPP for the indicated times & fixed. Cells were stained with antibodies against pS65-Ub (red) & the mitochondrial marker TOM20 (cyan). Scale bars correspond to 10 µM. (C) Quantification of Parkin translocation using High Content Imaging. HeLa EGFP-Parkin cells were treated for 4 or 8 h with or without 10 µM G-TPP. CCCP treatment (10 µM for 2 h) was used as a positive control. Cells were fixed, counterstained with Hoechst dye to visualize nuclei, imaged & analyzed using the ratio of cytoplasmic to nuclear EGFP signal [21]. Data was normalized to positive (2 h 10 µM CCCP treatment) & negative (2 h DMSO) controls. G-TPP significantly induced Parkin re-localization to levels similar to or beyond 2 h CCCP treatment. Shown are the mean values of three independent experiments with triplicate wells each ± SEM (one-way ANOVA with Tukey’s posthoc, ***p < 0.0005). Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.22287), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - G-TPP leads to recruitment of autophagy adapters & degradation of mitochondria(A) HeLa cells stably expressing untagged Parkin were treated with 10 µM G-TPP for 8 h. Western blots were prepared from cell lysates & probed with antibodies against LC3, phospho-TBK1 (Ser172) & TBK1. GAPDH was used as a loading control. Upon 8 h the levels of LC3-I & LC3-II were both increased. At 8 h after treatment with G-TPP but not at 4 or 24 h, TBK1 was phosphorylated. (B) HeLa cells stably expressing EGFP-Parkin were treated with 10 µM G-TPP & fixed 8 h after treatment. Cells were stained with antibodies against the autophagy adapter proteins NBR1, NDP52, OPTN, p62, & TAX1BP1 (red). Mitochondria were counterstained with TOM20 antibodies (cyan), nuclei with Hoechst (blue). EGFP-Parkin epifluorescence is shown in green. Scale bar corresponds to 10 µM. (C) HeLa cells stably expressing EGFP-Parkin & the reporter protein mitoKeima were treated with 10 µM CCCP or G-TPP & imaged over time. The ratio of ‘neutral’ mitoKeima to ‘acidic’ mitoKeima was calculated as readout for mitophagy. Parkin translocation was monitored at the same time. Values for Parkin translocation & mitophagy were normalized to 12 h treatment with 10 µM CCCP as positive control & DMSO as negative control (two-way ANOVA with Tukey’s post-hoc test, **p < 0.005, ***p < 0.0005). Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.22287), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: Rabbit Polyclonal PINK1 Antibody [BC100-494] - PINK1 detection in mouse and postmortem human cortex samples. 1:1000 dilution at 4 degrees overnight to detect endogenous PINK1 from mouse and postmortem human cortex samples (10 ug total protein). Image from a verified customer review.

Reactivity:

Hu, Mu, Rt, Rb

Species Glossary

Reactivity: Hu, Mu, Rt, Rb

Applications:

, , , , , , , , ,

Applications: , , , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	BC100-494AF350
Alexa Fluor 405	BC100-494AF405
Alexa Fluor 488	BC100-494AF488
Alexa Fluor 532	BC100-494AF532
Alexa Fluor 594	BC100-494AF594
Alexa Fluor 647	BC100-494AF647
Alexa Fluor 700	BC100-494AF700
Alexa Fluor 750	BC100-494AF750
Allophycocyanin	BC100-494APC
Biotin	BC100-494B
CoraFluor 1	BC100-494CL1
DyLight 350	BC100-494UV
DyLight 405	BC100-494V
DyLight 488	BC100-494G
DyLight 550	BC100-494R
DyLight 594	BC100-494DL594
DyLight 650	BC100-494C
DyLight 680	BC100-494FR
DyLight 755	BC100-494IR
FITC	BC100-494F
HRP	BC100-494H
Janelia Fluor 525	BC100-494JF525
Janelia Fluor 549	BC100-494JF549
Janelia Fluor 646	BC100-494JF646
Janelia Fluor 669	BC100-494JF669
PE	BC100-494PE
PerCP	BC100-494PCP
mFluor Violet 450 SE	BC100-494MFV450
mFluor Violet 500 SE	BC100-494MFV500
mFluor Violet 610 SE	BC100-494MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	BC100-494SS

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NBP1-40256

ATF6 Antibody (70B1413.1) - BSA Free

(3 Reviews)

(246 Publications)

0.1 mg

NBP1-40256

$<b>Biological Strategies Validation. </b>Western Blot: ATF6 Antibody (70B1413.1) [NBP1-40256] - Analysis of ATF6 in mouse liver tissue using 3 ug/ml of ATF6 antibody and 0.25 ug/ml of GAPDH antibody. Lane A contains 20 ugs of whole mouse liver lysate, lane B contains 20 ugs of total ER fraction, and lane C contains 20 ugs of rough ER fraction. The ATF6 band may represent under glycosylated or cleaved/active ATF6.$

Immunocytochemistry/Immunofluorescence: ATF6 Antibody (70B1413.1) [NBP1-40256] - Untreated HeLa cells were fixed in -20C methanol for 10 min, air dried and rehydrated in PBS at room temperature for 5 minutes. Cells were incubated with anti-ATF6 (1:20) for one hour at room temperature. ATF6 reactivity (green) was detected with anti-mouse Dylight-488 secondary antibody. Nuclei were counterstained with DAPI (blue). Note the ER localization of ATF6.

Immunohistochemistry-Paraffin: ATF6 Antibody (70B1413.1) [NBP1-40256] - Analysis of ATF6 antibody on Human placenta. Fixed paraffin-embedded sections. Antibody dilution 1:50. Incubated overnight in 4C. Image from verified customer review.

Flow (Intracellular): ATF6 Antibody (70B1413.1) [NBP1-40256] - An intracellular stain was performed on HeLa cells with ATF6 Antibody (70B1413.1) NBP1-40256F (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 10 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to FITC.. Using the FITC format of this antibody.

Western Blot: ATF6 Antibody (70B1413.1) [NBP1-40256] - Lane 1: 293 cells transfected with full-length ATF6. Lane 2: 293 cells transfected with partial length ATF6 (amino acids 1-373). Lane 3: Untransfected 293 cells. Western blots were probed with 4 ug/ml of the ATF6 monoclonal antibody and visualized with PicoTect Western Blot Chemiluminescence Substrate (10087K). Film was exposed for 1 min. The top arrow corresponds to the 90 kDa form of ATF6 described as full-length in the literature. The human full-length and partial length ATF6 plasmids are described in Luo and Lee (2002).

Immunohistochemistry-Paraffin: ATF6 Antibody (70B1413.1) [NBP1-40256] - Human placenta, followed by biotinylated horse anti-mouse IgG secondary antibody, alkaline phosphatase-streptavidin and chromogen. Dilution 10ug/ml

Flow Cytometry: ATF6 Antibody (70B1413.1) [NBP1-40256] - Intracellular flow cytometric staining of 1 x 10^6 MCF-7 cells using ATF6 antibody (dark blue). Isotype control shown in orange. An antibody concentration of 1 ug/1x10^6 cells was used.

Western Blot: ATF6 Antibody (70B1413.1) [NBP1-40256] - Lysate of DU145 cells. Image from verified customer review.

Western Blot: ATF6 Antibody (70B1413.1) [NBP1-40256] - Lysate of PC-3 cells. Image from verified customer review.

Expression of ER stress-associated transcription factors in NASH, NAFL and normal liver tissues beta -Actin was used as an internal control. Horizontal lines represent means of densitometry signals from the western blot analyses for all tissue groups. #, significant differences in signals between NASH and normal liver tissues (P < 0.05). Data for NAFL tissues were not used for statistical comparisons because of limited sample number (n = 2).

Abnormal Paneth cells show ER stress.(A, B) Representative transmission electron microscopy images of Paneth cells at the base of ileal crypts in (A) ICR & (B) SAMP1/YitFc mice. Scale bars indicate 2 μm. (C, D) Quantitative analysis of (C) granule number & (D) ER lumen diameter in Paneth cells (n = 3/each week for SAMP1/YitFc mice). For the measurements, three Paneth cells were randomly selected from each mouse. (E) SDS–PAGE Western blot analysis of ER stress markers, pIRE1 alpha , ATF4, cleaved-ATF6, & GRP78 in ileal crypts (n = 4/each group). Total-IRE1 alpha & HPRT1 was used as loading control. (F) Relative expression level of ER stress markers calculated from the band intensity. Error bars represent mean ± SEM. (C, D, F) Statistical significance was evaluated by t test in (C, D), & one-way ANOVA followed by Tukey’s post hoc test in (F). P < 0.05 was considered statistically significant. *P < 0.05, †P < 0.01, §P < 0.001. E, ER; G, granules; N, nucleus; n.s., not significant. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32345659), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ATF6 Antibody (70B1413.1) - BSA Free [NBP1-40256] - The ISR is active in the retinas of rd16 mice.Western blots & corresponding graphs of ISR markers in the retinas of rd16 mice at P15 (a) & P20 (b). At P15, p-eIF2 alpha , ATF4, CHOP, & TRB3 are significantly elevated. At P20, levels of p-eIF2 alpha , ATF4, CHOP, & GADD34 are increased. Markers of the UPR are elevated in rd16 retinas. BiP & cleaved (~50 kD) ATF6 are upregulated in the retinas of rd16 mice at P15 (c) & P20 (d). Relative density measurements correspond to the intensities of the immunoblotting bands or lanes normalized to an internal control. Data are shown as mean ± SEM. a.u. arbitrary units. P15 n = 3. P20 n = 4. *p < 0.05, **p < 0.01, ***p < 0.001 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29706649), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ATF6 Antibody (70B1413.1) - BSA Free [NBP1-40256] - Expression of ER stress-associated transcription factors in NASH, NAFL & normal liver tissues beta -Actin was used as an internal control. Horizontal lines represent means of densitometry signals from the western blot analyses for all tissue groups. #, significant differences in signals between NASH & normal liver tissues (P < 0.05). Data for NAFL tissues were not used for statistical comparisons because of limited sample number (n = 2). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28968997), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ATF6 Antibody (70B1413.1) - BSA Free [NBP1-40256] - Restoration of Plk3 induction rescues ATF2 phosphorylation & ER stress resolution in Lrh-1LKO mice, & loss or gain of ATF2 transcriptional activity also alters ER stress resolution capacity.(A) Primary hepatocytes prepared from Lrh-1f/fand Lrh-1LKO mice & transduced with Ad-Plk3 or Ad-control at a MOI of 100. Cells treated 36 hr later with vehicle or tunicamycin (TM) (0.01 µg/ml) & doxycycline (1 µg/ml) to induce Plk3 or LacZ control. Nuclear protein was obtained at timepoints indicated & immunoblotted for UPR transcription factors, with TBP as a loading control. Results representative of 3 independent experiments. Image collected & cropped by CiteAb from the following publication (//elifesciences.org/articles/01694), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ATF6 Antibody (70B1413.1) - BSA Free [NBP1-40256] - APPswe induction of OB-senescence via ER stress.a Heat map of differentially expressed ER stress or anti-stress related genes identified by RNA-seq in control (OCN-Cre; Ai9) & TgAPPsweOCN; Ai9 Td+ OB-progenitors (detail analysis was described in Methods). b RT-PCR analysis of ER stress-related genes Grp78, Atf6, Hsp90b1, Eif2ak3, Ern1, Hsp90aa1, & Hspa2 & anti-stress related gene Sirt3 gene expression in purified Td+ BMSCs from 6-MO control (OCN-Cre; Ai9) & TgAPPsweOCN; Ai9 mice, *p < 0.05, **p < 0.01, ***p < 0.001, mean ± SD, n = 3, Mann–Whitney U test. c Western blot analysis of indicated protein expression in BMSCs from mice with indicated genotypes (at 6-MO). GAPDH was used as a loading control. d Quantification of data in c, *p < 0.05, **p < 0.01. mean ± SD, n = 4, Student’s t test. e Western blot analysis of indicated protein expression in BMSCs from 6-MO control & TgAPPsweOCN with or without 0.25 mM 4-PBA (4-Phenylbutyric acid) treatment. f Quantification analyses of the data in e, *p < 0.05, n = 3. g SA-beta -gal staining of 6-MO control & TgAPPsweOCN BMSCs with vehicle (Veh)(PBS) & 4-PBA treatment, respectively, scale bar, 20 µm. h Quantification of SA-beta -gal+ cell densities in g (mean ± SD; n = 5, **p < 0.01, ***p < 0.001). Two-way analysis of variance test was used in f & h. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/34824365), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ATF6 Antibody (70B1413.1) - BSA Free [NBP1-40256] - Disturbance of ER homeostasis in ADTKD-UMOD.(A) ADTKD-UMOD is characterized by maturation & trafficking defect of mutant UMOD & intracellular accumulation of UMOD in TAL cells. UMOD immunolocalization revealed a diffuse cytoplasmic staining with enforcement of the luminal membrane in TAL cells of a wild-type mouse. In contrast, TAL cells of an UmodC93F mutant mouse displayed a strong paranuclear immunopositivity for UMOD. Wild-type: Umodwt mouse; UmodC93F: homozygous UmodC93F mutant mouse. Age of mice analysed: four months. Chromogen: DAB, nuclear staining: haemalum. (B) Heat map of relative expression values (z scores) showed differential abundance of several proteins localized in the ER. (C) In the outer medulla of Umod mutant mice of both mouse lines, a strong accumulation of immature UMOD was present. (D) Protein abundances of BiP, phospho-eIF2 alpha , eIF2 alpha , ATF4, both full-length (§) & cleaved activated (#) ATF6, & CHOP were increased in Umod mutant mice compared to wild-type mice. Signal intensities were corrected for GAPDH signal intensities of the same PVDF-membrane, which was stripped several times to facilitate the detection of multiple proteins. Mean of protein abundance of wild-type mice was set on a value of 1 [mean (wild-type) = 1]. Data are shown as means ± SD. One-way ANOVA with Newman-Keuls’s post hoc test: p vs. wild-type, *p < 0.05; **p < 0.01; ***p < 0.001. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/srep42970), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ATF6 Antibody (70B1413.1) - BSA Free [NBP1-40256] - The effect of Ezetimibe on unfolded protein response (UPR) gene expression in THP-1 cells exposed to ischemia-reperfusion (IR). (a) The mRNA expression of activating transcription factor 6 (ATF6) & CCAAT-enhancer-binding protein homologous protein (CHOP). (b) Representative Western blot analyses for the indicated proteins. (c,d) The average quantification of ATF6 & CHOP obtained by the densitometric analysis of three independent experiments. mRNA was analyzed by quantitative real-time PCR; normalized gene expression levels are given as the ratio between the mean value for the target gene & that for beta -actin in each sample. Data are expressed as mean ± SD. * p < 0.01 vs. control (up-regulation); ** p < 0.01 vs. IR; §p < 0.01 vs. control (down-regulation). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32340270), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: ATF6 Antibody (70B1413.1) - BSA Free [NBP1-40256] - Effect of rapamycin on markers of the UPR pathways(A) Cells were incubated in medium alone (0.05% FBS), with 3 nM IGF-1 or with both 3 nM IGF-1 & 10 nM rapamycin (IGF-1 + rapamycin). Total protein extracts prepared from cells incubated for 24 h in those conditions were subjected to Western Blot analysis. Protein expression levels were assessed for phosphorylated or total forms of PERK, eIF2 alpha & for CHOP, BiP, XBP1-s & XBP1-u proteins. Efficiency of rapamycin to inhibit mTORC1 pathway was also checked by immunoblot with phosphorylated & total forms of p70S6K1 & 4E-BP1. alpha -tubulin was used as internal control. (B & C) Cells were incubated with 10nM rapamycin for 1 h (B) or 24 h (C). Immunoblots for phosphorylated & total forms of PERK, eIF2 alpha , p70S6K1 & 4E-BP1 or for ATF4, CHOP, BiP, XBP1-s & XBP1-u protein expression were performed. alpha -tubulin was used as internal control. Blots of P-p70S6K1, p70S6K1, P-PERK, PERK, & alpha -tubulin of Figure 4B & blots of Figure 4C have been performed on the same electrophoresis gel, but cut & reconstituted. (D) Cells were incubated in medium alone (Ctrl) or with 10 nM rapamycin for 24 h. Nuclear localization of ATF6 was assessed using immunofluorescence with ATF6-antibody (red) & Hoechst dye. Magnification ×1000. (E) Bar graphs were obtained by quantification of ATF6 nuclear staining. Results are representative of at least 3 experiments. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.15469), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: ATF6 Antibody (70B1413.1) - BSA Free [NBP1-40256] - Activation of the UPR during hypoxia or glucose depletionSTC-1 & GluTag cells were subjected to hypoxia (1%) or cultivated with decreasing concentration of glucose i.e. 25, 5 or 1 mM, for 24 h. (A) & (C) Protein expression level of phosphorylated & total forms of PERK, eIF2 alpha & ATF4, CHOP, BiP & C-Caspase 3 protein expression was examined using immunoblots, during hypoxia (A) & glucose depletion (C). alpha -tubulin was used as internal control. Blots of Figure 2A have been performed on the same electrophoresis gel, but cut & reconstituted. (B) & (D) XBP1 mRNA splicing was analyzed by RT-PCR after Pst1 digestion: XBP1-u, unspliced; XBP1-h, hybrid; XBP1-s, spliced variant of XBP1; *, XBP1-u mRNA fragments after Pst1 digestion. (E) ATF6 nuclear localization was assessed in STC-1 cells using immunofluorescence with anti-ATF6 antibody & hoechst dye. Magnification x1000. Results are presentative of at least 3 independent experiments (A–E). (F) Bar graphs were obtained by quantification of ATF6 nuclear staining (*P < 0.05 versus control). Results are presentative of 3 independent experiments (A–E) or the mean ± S.E.M. of an experimental n = 3 (F). Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.15469), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: ATF6 Antibody (70B1413.1) - BSA Free [NBP1-40256] - UPR status in STC-1 & GluTag cell lines & effect of UPR inducers on markers of the UPR pathwaysSTC-1 & GluTag cells were incubated in medium (Ctrl) or ER stress-inducing agents thapsigargin (Tg, 300 nM), tunicamycin (Tn, 0.05 μg/mL) & brefeldin A (Bref A, 3 μM) for 4 h, 16 h & 8 h respectively. (A) Protein expression level of phosphorylated or total forms of PERK, eIF2 alpha & CHOP, BiP & cleaved-caspase 3 (C-Caspase 3) protein expression was examined using Western Blot analysis. alpha -tubulin was used as internal control (B) Densitometric quantification of P-PERK/PERK, P-eIF2 alpha /eIF2 alpha & BiP/ alpha -tubulin ratios analysis in STC-1 or GluTag cell lines (*P < 0.05 versus control). (C–D) The effect of Tg, Tn & Bref A on ATF6 nuclear localization was assessed by immunofluorescence in STC-1 cells (C) & GluTag cells (D) using anti-ATF6 antibody & Hoechst dye. Magnification ×1000. (E) Bar graphs obtained by quantification of ATF6 nuclear staining (*P < 0.05 versus control). (F) XBP1 mRNA splicing was analyzed by RT-PCR after Pst1 digestion: XBP1-h, hybrid, XBP1-u, unspliced; XBP1-s, spliced variant of XBP1; *, XBP1-u mRNA fragments after Pst1 digestion. Results are presentative of 3 independent experiments (A, C, D, F) or the mean ± S.E.M. of an experimental n = 3 (B, E). Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.15469), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ATF6 Antibody (70B1413.1) - BSA Free [NBP1-40256] - Tm‐induced UPR increases expression of RANKL in cultured osteoblastic & osteocytic cells. (A) Western blotting of cell lysates obtained from neonatal calvaria‐derived osteoblastic cells (Calvaria Ob) treated with 2.2 µg/mL Tm for the indicated times. (B‐D) Gene expression as determined by qRT‐PCR in (B) calvaria‐derived osteoblastic cells (n = 3/group) (C) Osteoblastic UAMS‐32 cells (UAMS‐32 Ob) (n = 4/group) or (D) osteocytic MLO‐Y4 cells (MLO‐Y4 Ot) (n = 4/group),maintained in presence of vehicle (, 0.1% DMSO) or 2.2 µg/ml Tm () for 4 hours. (E) Western blot of RANKL protein in cell lysates obtained from calvaria‐derived osteoblastic cells as described in A in a separate study. Data shown are the mean & SD with individual data points. *P < .05 vs vehicle by Student's t‐test Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32259048), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/Immunofluorescence: Mouse Monoclonal ATF6 Antibody (70B1413.1) [IMGENEX: IMG-273] [NBP1-40256] - Mice hepatocytes were stained for ATF6. Image from a verified customer review.

Western Blot: Mouse Monoclonal ATF6 Antibody (70B1413.1) [IMGENEX: IMG-273] [NBP1-40256] - Western blot of the mouse liver homogenates from control (1) and alcohol-fed mice (2). Image from a verified customer review.

Reactivity:

Hu, Mu, Rt, Po, Pl, Rb

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Pl, Rb

Applications:

, , , , , , , , ,

Applications: , , , , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Alt Catalog#

IMG-273

Alt Catalog# IMG-273

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NBP1-40256AF350
Alexa Fluor 405	NBP1-40256AF405
Alexa Fluor 488	NBP1-40256AF488
Alexa Fluor 532	NBP1-40256AF532
Alexa Fluor 594	NBP1-40256AF594
Alexa Fluor 647	NBP1-40256AF647
Alexa Fluor 700	NBP1-40256AF700
Alexa Fluor 750	NBP1-40256AF750
Allophycocyanin	NBP1-40256APC
Biotin	NBP1-40256B
CoraFluor 1	NBP1-40256CL1
DyLight 350	NBP1-40256UV
DyLight 405	NBP1-40256V
DyLight 488	NBP1-40256G
DyLight 550	NBP1-40256R
DyLight 594	NBP1-40256DL594
DyLight 650	NBP1-40256C
DyLight 680	NBP1-40256FR
DyLight 755	NBP1-40256IR
FITC	NBP1-40256F-0.1ml
HRP	NBP1-40256H
Janelia Fluor 525	NBP1-40256JF525
Janelia Fluor 549	NBP1-40256JF549
Janelia Fluor 646	NBP1-40256JF646
Janelia Fluor 669	NBP1-40256JF669
PE	NBP1-40256PE
PerCP	NBP1-40256PCP
mFluor Violet 450 SE	NBP1-40256MFV450
mFluor Violet 500 SE	NBP1-40256MFV500
mFluor Violet 610 SE	NBP1-40256MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NBP1-40256SS
Azide and BSA Free	NBP2-80583

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(select up to 3 products from this page to compare)

NB100-56708

Caspase-3 Antibody (31A1067) - (Pro and Active) - BSA Free

(2 Reviews)

(202 Publications)

0.1 mg

NB100-56708

Image of Caspase-3 Antibody (31A1067) - (Pro and Active). Whole cell protein from Jurkat cells treated with and without 2 uM staurosporine as indicated was separated on a 4-15% gel by SDS-PAGE, transferred to 0.2 um PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with 5 ug/ml anti-Caspase 3 in 1% milk, and detected with an anti-mouse HRP secondary antibody using a Femto sensitivity chemiluminescence reagent. Note the detection of both pro-caspase 3 at 35 kDa and the cleaved active caspase 3 at 15-17 kDa.

<b>Biological Strategies Validation. </b>Tissue section of human spleen using 1:200 dilution of Caspase-3 antibody (clone 31A1067). The staining was developed with HRP labeled anti-mouse IgG secondary antibody and DAB reagent, and nuclei of cells were counter-stained with hematoxylin. This Caspase 3 antibody generated primarily a specific cytoplasmic staining in a subset of spleenocytes with some nuclear signal in a few cells.

Simple Western lane view shows a specific band for Caspase-3 Antibody (31A1067) - (Pro and Active) in 0.1 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230kDa separation system.

Caspase-3 was detected in immersion fixed paraffin-embedded sections of human bladder tissue using 1:50 dilution of mouse aCaspase-3 Antibody (31A1067) - (Pro and Active) (NB100-56708), for 1 hour at room temperature followed by anti-mouse IgG VisUCyte HRP polymer(VC001). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue).

Paclitaxel in combination with MWE retarded tumor growth in a human bladder carcinoma TSGH 8301 xenograft model. The levels of total (t-PTEN) and phospho-PTEN (p-PTEN) and Caspase 3 in the tumor specimens were determined by Western blotting and then quantified using beta-actin as the protein loading control; the results are expressed as a percentage of the control. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep20417), licensed under a CC-BY license.

An intracellular stain was performed on NIH3T3 cells with Caspase-3 Antibody (31A1067) - (Pro and Active) Antibody NB100-56708AF700 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 10 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 700.

<b>Biological Strategies Validation. </b>Lysates of Jurkat human acute T cell leukemia cell line untreated (-) or treated (+) with VP-16. PVDF membrane was probed with 0.1 ug/mL of mouse monoclonal Caspase-3 Antibody (31A1067) - (Pro and Active) (NB100-56708, Novus Biologicals) followed by 1:2000 dilution donkey anti-mouse IgG.

An intracellular stain was performed on HeLa cells with Caspase-3 Antibody (31A1067) - (Pro and Active) NB100-56708 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature, followed by mouse F(ab)2 IgG (H+L) APC-conjugated secondary antibody (F0101B, R&D Systems).

Western Blot: Mouse Monoclonal Caspase-3 Antibody (31A1067) - (Pro and Active) [IMGENEX: IMG-144A] [NB100-56708] - Whole cell lysates from MDA-MB-231, MCF-7, SUM149 and SUM159 cells were loaded with 50 ug/lane. 10% SDS-PAGE. Caspase-3 Antibody (NB100-56708) was used for primary antibody: 1:2000, 4℃, overnight. Image from a verified customer review.

Immunocytochemistry/ Immunofluorescence: Caspase-3 Antibody (31A1067) - (Pro and Active) - BSA Free [NB100-56708] - rOPN administration influenced the interaction & balance between Beclin 1 & Caspase‐3 at 24 h after SAH. Double immunofluorescence staining of Caspase‐3 & Beclin 1 in Sham group, SAH + Vehicle group & SAH + rOPN group at 24 h after SAH induction. Sample size is 9, n = 3 per group. Localization of Caspase‐3 can be cytoplasmic & nuclear. Staining in the nucleus is considered to be an indication of active Caspase‐3. The dashed lines & the red box on brain slice images indicate the locations observed. Vehicle, phosphate‐buffered saline; Scale bar = 50 μm Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31436915), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: Caspase-3 Antibody (31A1067) - (Pro and Active) - BSA Free [NB100-56708] - PEM induces YIPF2 upregulation & apoptosis in NSCLC cells.a, b H1792 (a) & H1299 (b) NSCLC cells were treated with PEM at various concentrations (0–10.0 μM) for 36 h. Cell lysates were analyzed by Western blotting with antibodies against YIPF2 & ACTB. c Overexpression of YIPF2 in H1299 cells in the presence or absence of PEM at 5.0 μM for 36 h. Cell lysates were analyzed by Western blotting with antibodies against YIPF2, CASP8, CASP3, PARP1 & ACTB. d Knockdown of YIPF2 expression by YIPF2–1 siRNA in A549 NSCLC cells in the presence or absence of PEM at 5.0 μM for 36 h. Cell lysates were analyzed by Western blotting with antibodies against YIPF2, CASP8, CASP3, PARP1 & ACTB. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32303681), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: Caspase-3 Antibody (31A1067) - (Pro and Active) - BSA Free [NB100-56708] - Lipofection of top broccoletti-miR candidates does not influence basal & induced apoptosis.(A) BxPc-3 & Bx-Gem cells were transfected as described in Figure 3. Seventy-two hours later, the cells were stained with Annexin V-PE & 7-AAD, followed by FACS analysis. The percentage of Annexin V- & 7-AAD-positive cells is shown. (B) Lipofected BxPc-3 & Bx-Gem cells were stained with an antibody specific for the proliferation marker Ki-67 (green) or the apoptosis marker cleaved fragment of caspase-3 (red), which indicates apoptosis. Representative images at ×100 magnification are shown. The percentage of Ki-67- or caspase-3-positive cells was counted in 18 visual fields, & the means ± SD are shown in the diagram below. (C) BxPc-3 & Bx-Gem were lipofected as described above, & at 24 h later, the cells were treated with gemcitabine (10 nM) or were left untreated. Ninety-six hours after gemcitabine treatment, viability was determined by MTT assay. The data are presented as the means ± SD (**P < 0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32292571), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: Caspase-3 Antibody (31A1067) - (Pro and Active) - BSA Free [NB100-56708] - PEM induces apoptosis of NSCLC cells via YIPF2-TNFRSF10B axis.a, b A549 (a) & H1792 (b) cells were treated with PEM at 5.0 μM for the indicated times (0, 6, 12, 24, 36 & 48 h). Cell lysates were analyzed by Western blotting with antibodies against YIPF2, TNFRSF10B & ACTB. c A549 cells were treated with doxorubicin (DOX) at various concentrations (0–2.0 μM) for 18 h. Cell lysates were analyzed by Western blotting with antibodies against YIPF2, TNFRSF10B & ACTB. d Overexpression of YIPF2 in H1792 & H1299 cells in the presence or absence of PEM at 5.0 μM for 36 h. Cell lysates were analyzed by Western blotting with antibodies against YIPF2, TNFRSF10B & ACTB. e Knockdown of YIPF2 expression by YIPF2–1 siRNA in A549 & H1792 cells in the presence or absence of PEM at 5.0 μM for 36 h. Cell lysates were analyzed by Western blotting with antibodies against YIPF2, TNFRSF10B & ACTB. f Overexpression of YIPF2 in H1299 cells (left) or Knockdown of YIPF2 expression by YIPF2–1 siRNA in H1792 cells (right) in the presence or absence of PEM at 5.0 μM for 36 h. Cell lysates were analyzed by Western blotting with antibodies against YIPF2, TNFRSF10A & ACTB. g Three A549 cell lines (Ctrl, YIPF2, YIPF2 + siTNFRSF10B) in the presence or absence of PEM at 5.0 μM for 36 h. Cell lysates were analyzed by Western blotting with antibodies against YIPF2, TNFRSF10B, CASP8, CASP3 & ACTB. h Three H1299 cell lines (Ctrl, siYIPF2–1, siYIPF2–1 + TNFRSF10B (short isoform)) in the presence or absence of PEM at 5.0 μM for 36 h. Cell lysates were analyzed by Western blotting with antibodies against YIPF2, TNFRSF10B, CASP8, CASP3 & ACTB. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32303681), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: Caspase-3 Antibody (31A1067) - (Pro and Active) - BSA Free [NB100-56708] - Cell numbers positively stained for NeuN, DCX, PCNA & caspase-3 in the subgranular region of the dentate gyrus in WT & RanBP9−/− (KO) mice.(A), DAPI-stained brain sections to show the highlighted subgranular zone within the dentate gyrus region of the hippocampus used for cell counts shown in B. (B), Representative brain sections stained with anti-NeuN, anti-DCX, anti-PCNA, anti-capsase-3 & counter stained with DAPI. Cell counting revealed significantly decreased numbers of NeuN positive cells in RanBP9−/− (KO) brains (22%) compared to WT controls. However DCX, PCNA & caspase positive cell numbers were not significantly altered. In each group, n = 3, data presented as mean± SEM. **, p<0.01 by Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23840553), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: Caspase-3 Antibody (31A1067) - (Pro and Active) - BSA Free [NB100-56708] - NFATc1 regulates DcR3 expression at a transcriptional level. (A,B) Immunoblot analysis of whole-cell lysates & quantitative real-time-PCR assaying relative DcR3 mRNA expression of ACHN & 769-P cells 24 h after treatment with cyclosporin A (CsA, 25 μM) or Tacrolimus (FK-506, 50 μM) (A); 48 h post transfection with NFATc1 or an empty vector control (neo) (B). Expression data were normalized to internal 18S rRNA expression (mean ± SEM; n=3; *p<0.05, **p<0.01, ***p<0.001; T-test). (C) Immunoblot analysis of cytoplasmic & nuclear fractions of ACHN & 769-P cells after treatment with LY294002 (50 μM), Everolimus (1 μM), or Cyclosporine A (25 μM). (D) Relative NFATc1–luciferase reporter activity of ACHN & 769-P cells 24 h post transfection with myrAkt or an empty vector control (neo) (mean ± SEM; n=3; *p<0.05, **p<0.01; T-test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24107265), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: Caspase-3 Antibody (31A1067) - (Pro and Active) - BSA Free [NB100-56708] - rOPN administration elevated the expression of autophagy‐related proteins while suppressing apoptosis in rat brain at 24 h after SAH. The effects of rOPN on expression levels of (A) Beclin 1, mean ± SD is 1.016 ± 0.2262 in Sham group, 2.874 ± 1.147 in SAH + Vehicle group, 4.963 ± 2.05 in SAH + rOPN group, F = 15.52, (B) ATG5, mean ± SD is 0.8908 ± 0.2545 in Sham group, 2.332 ± 0.6431 in SAH + Vehicle group, 4.364 ± 1.309 in SAH + rOPN group, F = 25.02, (C) LC3, mean ± SD is 1 ± 0.1845 in Sham group, 1.755 ± 0.3017 in SAH + Vehicle group, 2.7 ± 0.7957 in SAH + rOPN group, F = 17.23, (D) Cleaved Caspase‐3, mean ± SD is 1.008 ± 0.186 in Sham group, 4.112 ± 1.528 in SAH + Vehicle group, 2.291 ± 0.6268 in SAH + rOPN group, F = 15.86, (E) Bax, mean ± SD is 1.006 ± 0.321 in Sham group, 37.47 ± 10.86 in SAH + Vehicle group, 23.83 ± 8.143 in SAH + rOPN group, F = 33.13, (F) Bcl‐2, mean ± SD is 1.005 ± 0.2736 in Sham group, 0.2309 ± 0.1257 in SAH + Vehicle group, 0.7843 ± 0.2278 in SAH + rOPN group, F = 20.1, in the left hemisphere of rat brain at 24 h after SAH. Sample size is 18, n = 6 per group. Data were presented as mean ± SD. *P < .05, ***P < .001 vs Sham group; #P < .05, ##P < .01 vs SAH + Vehicle group Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31436915), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: Caspase-3 Antibody (31A1067) - (Pro and Active) - BSA Free [NB100-56708] - RAB8 suppresses PEM-induced apoptosis of NSCLC cells by promoting the removing of TNFRSF10B from plasma membrane to cytoplasm.a, b Knockdown of RAB8 expression by RAB8 siRNA in H1792 (a) & A549 (b) cells in the presence or absence of PEM at 5.0 μM for 36 h. The surface expression of TNFRSF10B was confirmed by flow cytometry analyses. c Overexpression of RAB8 in H1299 cells in the presence or absence of PEM at 5.0 μM for 36 h. Cell lysates were analyzed by Western blotting with antibodies against RAB8, TNFRSF10B, CASP8, CASP3, PARP1 & ACTB. d Knockdown of RAB8 expression by RAB8 siRNA in H1792 cells in the presence or absence of PEM at 5.0 μM for 36 h. Cell lysates were analyzed by Western blotting with antibodies against RAB8, TNFRSF10B, CASP8, CASP3, PARP1 & ACTB. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32303681), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Ch, ChHa, Ma

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Ch, ChHa, Ma

Applications:

, , , , , , , , , , ,

Applications: , , , , , , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Alt Catalog#

IMG-144A

Alt Catalog# IMG-144A

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-56708AF350
Alexa Fluor 405	NB100-56708AF405
Alexa Fluor 488	NB100-56708AF488
Alexa Fluor 532	NB100-56708AF532
Alexa Fluor 594	NB100-56708AF594
Alexa Fluor 647	NB100-56708AF647
Alexa Fluor 700	NB100-56708AF700
Alexa Fluor 750	NB100-56708AF750
Allophycocyanin	NB100-56708APC
Biotin	NB100-56708B
CoraFluor 1	NB100-56708CL1
DyLight 350	NB100-56708UV
DyLight 405	NB100-56708V
DyLight 488	NB100-56708G
DyLight 550	NB100-56708R
DyLight 594	NB100-56708DL594
DyLight 650	NB100-56708C
DyLight 680	NB100-56708FR
DyLight 755	NB100-56708IR
FITC	NB100-56708F
HRP	NB100-56708H
Janelia Fluor 525	NB100-56708JF525
Janelia Fluor 549	NB100-56708JF549
Janelia Fluor 646	NB100-56708JF646
Janelia Fluor 669	NB100-56708JF669
PE	NB100-56708PE
PerCP	NB100-56708PCP
mFluor Violet 450 SE	NB100-56708MFV450
mFluor Violet 500 SE	NB100-56708MFV500
mFluor Violet 610 SE	NB100-56708MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-56708SS
Azide and BSA Free	NBP2-33244

compare

(select up to 3 products from this page to compare)

NB100-56875

GAPDH Antibody - BSA Free

(5 Reviews)

(131 Publications)

0.1 mg

NB100-56875

$Western Blot: GAPDH Antibody [NB100-56875] - Analysis of GAPDH using this antibody at 1:500 in nuclear and cytoplasmic fractions made from Drosophila head extracts. Data courtesy of Dr. Jerry Lin, University of Wisconsin-Madison.$

Western Blot: GAPDH Antibody [NB100-56875] - Analysis using HeLa cells. Theoretical molecular weight: 36 kDa.

$Western Blot: GAPDH Antibody [NB100-56875] - Vps13 co-fractionates with Rab7 and Rab5. Western blot analysis of control fly head samples fractionated into a cytosolic and membrane fraction from postnuclear supernatant (PNS). EGFR was used as a membrane marker and GAPDH as a cytosolic marker. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0170106), licensed under a CC-BY license.$

Western Blot: GAPDH Antibody [NB100-56875] - Particle-induced Changes in Apoptosis are Restored by Firoin. Peripheral blood neutrophils from healthy donors (n57), 2 h pre-treated with indicated amounts of firoin (F) or 1 mM ectoine (E) before CNP exposition (33 mg/ml). : 6 h post CNP-treatment the anti-apoptotic Mcl-1 expression was measured by Western blot analysis. GAPDH was used as a loading control. Two representative blots from different individuals are shown and irrelevant lanes were removed. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0111485), licensed under a CC-BY license.

Simple Western: GAPDH Antibody [NB100-56875] - Lane view shows a specific band for GAPDH in 0.5 mg/ml of HeLa lysate. This experiment was performed under reducing A246conditions using the 12-230 kDa separation system. Note: band observed higher than predicted 36 kDa molecular weight.

$Western Blot: GAPDH Antibody [NB100-56875] - Vps13 co-fractionates with Rab7 & Rab5.(A) Western blot analysis of control fly head samples fractionated into a cytosolic & membrane fraction from postnuclear supernatant (PNS). EGFR was used as a membrane marker & GAPDH as a cytosolic marker. (B) Membrane fractions from control fly heads treated with 1 M KCl, Na2CO3 pH 11 or 6 M urea were centrifuged to separate the soluble & insoluble (membrane containing) fractions. The level of Vps13 was determined in these fractions. Markers for peripheral membrane proteins (GM130), integral membrane proteins (EGFR) & the cytosolic proteins (GAPDH) were used. The “Vps13 lysate” lane contains a lysate derived from Vps13 homozygous mutant fly heads, as expected no Vps13 is detected, demonstrating the specificity of the antibody against Vps13. (C) Membranes from control fly heads were fractionated on a sucrose gradient. Western blot analysis was performed to analyze the distribution of Vps13 in relation to markers associated with membranes of various organelles: Rab7 (late endosomes), Rab5 (early endosomes), GM130 (golgi), Lamp1 (lysosomes) & ATP5A (mitochondria). (D) Immunoisolation of membranes from fraction 14 of the sucrose gradient using Vps13 NT, Rab7 & Rab5 antibodies. (E) Quantification of the sucrose gradient fractionation of Fig 2C. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28107480), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

$Western Blot: GAPDH Antibody [NB100-56875] - Overexpression of HsVps13A rescues phenotypes of Vps13 mutants.(A) Samples from fly heads of Actin-GAL4 / + (as a control) & Actin-GAL4 / UAS-HsVps13A (HsVps13A expressing) flies were separated into a membrane & cytosol fraction & analyzed by Western blot for HsVps13A levels. EGFR & GAPDH used as controls for membrane & cytosolic proteins, respectively. (B) Eclosion rate of Vps13 mutant flies a Actin-GAL4/+ (control) or Actin-GAL4/UAS-HsVp13A (HsVps13A expressing) background at 25°C. (C) Ubiquitylated proteins from samples of 1 day old fly head extracts of Vps13/CyO; Actin-GAL4/+ (as a control), Vps13/ Vps13; Actin-GAL4/+ (representing homozygous mutants) & Vps13/ Vps13; Actin-GAL4/UAS-HsVps13A (representing homozygous mutants expressing human VPS13A). (D) Representative picture of ubiquitylated protein staining of the third instar larval ventral nerve cord of Vps13/CyO; Actin-GAL4/+ (as a control), Vps13/ Vps13; Actin-GAL4/+ & Vps13/ Vps13; Actin-GAL4/UAS-HsVps13A. Arrows indicate accumulations of ubiquitylated positive structures. The scale bar indicates 50 μm & 12,5 μm in the enlargement. (E) Quantification of the number of puncta in third instar larval ventral nerve cord of the experiment presented in Fig 6D. (F) Life span curve of Vps13/ Vps13; Actin-GAL4/+ & Vps13/ Vps13; Actin-GAL4/UAS-HsVps13A. All quantifications show the mean & SEM of at least three independent experiments per condition. For statistical analysis a two-tailed students T-test was used in combination with a Welch’s correction if necessary. P<0.05 is *, P<0.01 is ** & P<0.001 is ***. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28107480), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: GAPDH Antibody [NB100-56875] - No dystrophin expression was detected in cardiac & skeletal muscles of Dmdmdx rats.(A) Male 7 month-old rats of line 61, wild-type littermate controls (WT) & Dmdmdx were sacrificed & biopsies from tibialis cranialis muscles (TC) & hearts (H) were harvested. Western-blot of total proteins (50 µg) was incubated with NCL-DYS2 & Manex1011C monoclonal antibodies (C-terminal & exons 10/11 epitopes, respectively). This revealed undetectable levels of the 427 kDa dystrophin band in line 61 Dmdmdx rats. Muscle from a GRMD dog (GD) was used as negative control & samples from WT rats were used as positive controls. Staining with an anti-GAPDH polyclonal antibody validated equal protein loadings. (B–E) Heart & biceps femoris muscles from the same wild-type (B & C) & Dmdmdx rats (D & E) were assessed for dystrophin expression using immunohistochemistry with Mandys110 monoclonal antibody (against exons 38–39 epitope). Compared to the subsarcolemmal expression of dystrophin in wild-type muscles, no dystrophin was detected in Dmdmdx rats except for the presence in skeletal muscle of only rare scattered revertant positive fibers (arrowheads). Immunolabelling of dystrophin (B–E) Bar = 100 µm. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0110371), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody [NB100-56875] - ABCA1, ABCG1 & SR-BI protein expressions. a & b Hepatic protein expressions of ABCA1, ABCG1 & SR-BI were significantly decreased in COMT−/− mice at GD 18.5, compared to C57BL/6 J mice. Decreased hepatic ABCA1 expression was also observed at 10 days postpartum. ATI-5261 increased ABCA1 & ABCG1 expression in the liver at 10 days postpartum. c Placental protein expressions of ABCA1 & ABCG1 was reduced in COMT−/− mice, compared to C57BL/6 J mice. ATI-5261 treatment significantly increased ABCA1 levels in the placenta of COMT−/− mice. d Representative immunoblots of the corresponding proteins in the placenta with mouse RAW264.7 cell lysate included as positive control. Similar results were obtained when the experiment was repeated with lysates prepared from three batches of tissues. Data are presented as mean ± SEM. Groups (n = 8 in all groups) were compared using one-way ANOVA with post-hoc analysis (Tukey’s procedure). *, p < 0.05 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30237900), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: GAPDH Antibody [NB100-56875] - Vps13 co-fractionates with Rab7 & Rab5.(A) Western blot analysis of control fly head samples fractionated into a cytosolic & membrane fraction from postnuclear supernatant (PNS). EGFR was used as a membrane marker & GAPDH as a cytosolic marker. (B) Membrane fractions from control fly heads treated with 1 M KCl, Na2CO3 pH 11 or 6 M urea were centrifuged to separate the soluble & insoluble (membrane containing) fractions. The level of Vps13 was determined in these fractions. Markers for peripheral membrane proteins (GM130), integral membrane proteins (EGFR) & the cytosolic proteins (GAPDH) were used. The “Vps13 lysate” lane contains a lysate derived from Vps13 homozygous mutant fly heads, as expected no Vps13 is detected, demonstrating the specificity of the antibody against Vps13. (C) Membranes from control fly heads were fractionated on a sucrose gradient. Western blot analysis was performed to analyze the distribution of Vps13 in relation to markers associated with membranes of various organelles: Rab7 (late endosomes), Rab5 (early endosomes), GM130 (golgi), Lamp1 (lysosomes) & ATP5A (mitochondria). (D) Immunoisolation of membranes from fraction 14 of the sucrose gradient using Vps13 NT, Rab7 & Rab5 antibodies. (E) Quantification of the sucrose gradient fractionation of Fig 2C. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28107480), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Simple Western: GAPDH Antibody [NB100-56875] - Analysis of non-canonical inflammasome pathway.A LDH cytotoxicity assay in the presence of LPS or SCGB3A2 alone, or the two together (SCGB3A2 + LPS). B LDH cytotoxicity assay in the presence of various amount of nigericin. Average ± SD from more than three independent experiments. *P < 0.01, **P < 0.0001 by Tukey’s multiple comparison. C Morphology of cells cultured in the presence of LPS or SCGB3A2 alone, SCGB3A2 + LPS, or nigericin for 3 h. For nigericin-treated group, cells were primed with LPS before addition of nigericin. Black arrow indicates ballooned cells, characteristic feature of pyroptosis. D Western blotting for the cleaved forms of CASP1 (p20), CASP4 (p20), & GSDMD (N-terminal). S: SCGB3A2, N: nigericin. Experiments were repeated more than twice & same results were obtained. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33452234), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Ca, Dr, Fe, Ha, Pm, Ma

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Ca, Dr, Fe, Ha, Pm, Ma

Applications:

, , , ,

Applications: , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Alt Catalog#

IMG-5143A

Alt Catalog# IMG-5143A

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-56875SS

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NB100-137

EGLN1/PHD2 Antibody - BSA Free

(12 Reviews)

(96 Publications)

0.1 mg

NB100-137

Western Blot: EGLN1/PHD2 Antibody [NB100-137] - Analysis of PHD2 expression in human prostate cancer cell lines. Western blot image submitted by a verified customer review.

Immunocytochemistry/Immunofluorescence: EGLN1/PHD2 Antibody [NB100-137] - Staining of endogenous PHD2 in U2OS cells. ICC/IF image submitted by a verified customer review.

<b>Genetic Strategies Validation. </b>Western Blot: EGLN1/PHD2 Antibody [NB100-137] - Detection of PHD2 in human glioblastoma cell lysates. Image submitted by a verified customer review.

Western Blot: EGLN1/PHD2 Antibody [NB100-137] - Detection of human PHD2 by Western blot. Recombinant epitope-tagged PHD1, PHD2 or PHD3 (10 ng/lane) or whole cell lysate from HeLa cells. EGLN1/PHD2 antibody used at 1 ug/mL. Detection by chemiluminescence.

Immunohistochemistry: EGLN1/PHD2 Antibody [NB100-137] - EGLN1/PHD2 and EGFR expression levels positively correlate in breast cancer. Processed tissue microarrays of breast cancer biopsies from 313 patients were stained with EGLN1/PHD2 and EGFR antibodies. Four representative immunohistochemistries of human breast cancer with low and high expression of EGLN1/PHD2 and EGFR are shown. Magnification 10x. Image collected and cropped by CiteAb from the following publication (//www.oncotarget.com/article/14241/text/) licensed under a CC-BY license.

Western Blot: EGLN1/PHD2 Antibody [NB100-137] - Exogenous PHD2 has no impact on the gene expression of HIF-1alpha and HIF-2alpha. U87MG cells were transfected with empty vector (pcDNA) or PHD2 plasmid. Twenty-four hours after transfection, PHD2 was detected by immunoblotting. beta-Actin was used as loading control. The results are representative for three independent experiments. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/cddis2014295), licensed under a CC-BY license.

Flow Cytometry: EGLN1/PHD2 Antibody [NB100-137] - An intracellular stain was performed on Jurkat cells with NB100-137AF647 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.

Western Blot: EGLN1/PHD2 Antibody [NB100-137] - Analysis of PHD2 in normoxia (lane 1) or hypoxia (lane 2) treated SK-N-BE(2) cells using anti-EGLN1/PHD2 antibody. Western blot image submitted by a verified customer review.

Immunocytochemistry/Immunofluorescence: EGLN1/PHD2 Antibody [NB100-137] - Staining of PHD2 in HeLa cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red).

Immunohistochemistry: EGLN1/PHD2 Antibody [NB100-137] - Staining of lung vascular endothelium with EGLN1/PHD2 antibody. Image at 40X.

Flow Cytometry: EGLN1/PHD2 Antibody [NB100-137] - Detection of PHD2 in Jurkat cells. One million Jurkat cells were fixed, permeabilized, and stained with 3.0 ug/mL anti-EGLN1/PHD2 antibody in a 150 uL reaction. Isotype control (black), anti-MLL1 (red).

PHD2 and EGFR expression levels positively correlate in breast cancerProcessed tissue microarrays of breast cancer biopsies from 313 patients were stained with PHD2 and EGFR antibodies (cf Materials and methods). Four representative immunohistochemistries of human breast cancer with low and high expression of PHD2 and EGFR are shown. Magnification 10x.

Initial characterization of the OS-9 protein.(A) OS-9 expression in various human cell lines. Equal protein amounts of total cell lysates were used for SDS-PAGE & subsequent Western blotting. For each cell line, two independent samples are shown. Endogenous OS-9 was detected with a polyclonal antibody raised against a peptide corresponding to amino acids 600–667 of isoform 1 of OS-9. (B) Protein stability assay of endogenous OS-9. U2OS cells were treated with the translational inhibitor cycloheximide (100 µM). At indicated time points, whole cell lysates were analysed by immunoblotting. (C) Effect of hypoxia on OS-9 expression. For hypoxia, UT-7 cells were exposed to 1% O2 for 24 h prior to Western blot analysis. To determine any influence of HIF-1 alpha on OS-9 expression under normoxia, cells were incubated with the prolyl hydroxylase inhibitor DMOG (0.5 mM) for 24 h. (D) Protein interaction between OS-9 & PHD2 in vitro. For co-immunoprecipitation, U2OS cells were transiently co-transfected with the plasmids pOS-9-V5 & pPHD2-His, lysed in NP40 buffer, & subjected to immunoisolation with anti-V5 antibody recognizing OS-9 by its V5-tag. OS-9 & its associated proteins were separated by SDS-PAGE & analyzed by Western blot (lane 2). As controls, samples of untransfected (lane 1) cells or cells transfected with a single plasmid (lanes 3–4) were loaded. Representative Western blots are shown for each subfigure. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/21559462), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Cellular localization of OS-9 & PHD2.(A) A lectin gel-shift assay was conducted to test for glycosylated proteins. Total cell lysates of U2OS cells were incubated in the presence or absence of the endoglycosidases EndoH & PNGaseF for 6 h at 37°C. Digest products were separated on a reducing 10% SDS-PAGE gel which contained concanavalin A co-polymerized in the top layer of the separating gel to retard mobility of glycosylated proteins [56]. Glycosylated OS-9 is indicated as ‘g’, deglycosylated OS-9 as ‘d’. (B) Detection of OS-9 & PHD2 in the nuclear fraction. HEK293 cells with & without transfection of the plasmid pcDNA3-OS-9 were separated into nuclear fraction (N) & postnuclear supernatant (PS), the latter containing cytoplasm & organelles. Western blot analysis included BiP, GAPDH & lamin A as typical marker proteins for the ER, the cytoplasm & the nucleus, respectively. (C) Detection of OS-9 & PHD2 in the cytoplasm. HEK293 cells were co-transfected with pcDNA3-OS-9 & pPHD2-V5. For hypoxia, cells were exposed to 3% O2 for 4 h. Cells were treated with 50 µg/ml digitonin & centrifuged to obtain a cytoplasmic (C) & an organelle fraction (O) & subjected to immunoblotting. (D) Isolation of cellular endomembranes. HEK293 cells were lysed mechanically by several passages through a 30½G needle. The postnuclear supernatant was processed further by ultra-centrifugation to separate the organelles (O) from the cytosol (C). High salt treatment (1 M KCl) of the organelle fraction produced a wash fraction (W) that contained dissociated peripheral membrane proteins. For immunoblot analysis of subcellular fractionations, cell aliquots were normalized for cell number prior to loading (B–D). Representative Western blots are shown for each subfigure. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/21559462), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: EGLN1/PHD2 Antibody [NB100-137] - Representative picture of western blot in histopathologically unchanged tissue (N) & primary cancerous tissue (C) from patients with CRC. Immunodetection of bands was performed with Rp anti- PHD1, - PHD2, - PHD3 & - FIH Ab, followed by incubation with goat anti-rabbit HRP-conjugated Ab. The membrane was stripped & incubated with Rp anti-GAPDH Ab, followed by incubation with goat anti-rabbit HRP-conjugated Ab. Bands were revealed using SuperSignal West Femto Chemiluminescent Substrate, Thermo Fisher Scientific (Rockford, IL) & Biospectrum® Imaging System 500, UVP Ltd. (Upland, CA). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24195777), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: EGLN1/PHD2 Antibody [NB100-137] - OS-9 shows no effect on regulation of HIF-1 alpha .Total cell lysates were used for SDS-PAGE & subsequent Western blotting. To generate nearly anoxic conditions, cells were exposed to an oxygen consuming chemical system or to 1% or 3% O2 for 4 h to generate hypoxia. (A) U2OS, HeLa & Hep3B cells were transiently transfected with the plasmid pOS-9-V5 48 h prior to the experiment. Lamin A & actin were used as loading controls. (B) U2OS cells were subjected to ER stress by incubation either with tunicamycin (1 µg/ml) or thapsigargin (0.5 µg/ml) for 20 h. To detect HIF-1 alpha under normoxia, cells were treated with DMOG (1 mM) for 4 h. A sample of DMSO-only treated cells was loaded to exclude unspecific side effects of the solvent. (C) U2OS cells were transduced with lentiviral construct pLKO.1-shRNA-OS-9 (shOS-9) mediating a stable knockdown of OS-9 expression. Control cells (c) were transduced with plasmid pLKO.1-puro. Representative Western blots are shown for each subfigure. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/21559462), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: EGLN1/PHD2 Antibody [NB100-137] - Oxygen chemotaxis is independent of the PHD/HIF pathway. a–dHIF1A, HIF2A, HIF1A+HIF2A & PHD2 CRISPR/Cas9 KO clones characterisation, respectively, regarding O2-directed migration. Left panels: immunoblot validation of HIF1A, HIF2A, HIF1A+HIF2A & PHD2 KO clones. To blot HIFs factors (a, b, c), cells were first pre-treated for 5 h with CoCl2 300 µM before protein extraction, a condition that promotes HIF factors accumulation (cf. Supplementary Fig. 8f). Middle panels: cell trajectories under confinement. Red dashed lines indicate the border of the cell cluster at 0 h. Right panels: relative distribution of MCF10A KO clones versus wt cells at the edge of the cluster at 48 h. These experiments demonstrate that HIF factors deletion does not prevent aerotaxis. e, f Tracks & redistribution of wt & PHD2 KO clone silenced for PHD3 (siPHD3) or not (siCTR). g Tracks & redistribution of MCF10A cells treated with DMOG (50 µM) or CoCl2 (50 µM) to inhibit PHDs, or with vehicle only (DMSO). These experiments demonstrate that PHDs do not participate in O2-sensing during aerotaxis. Confinement was applied for 48 h (a–g). Scale bars, 500 µm Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30382089), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: EGLN1/PHD2 Antibody [NB100-137] - PHD3 expression correlates with a mesenchymal-like morphology in pancreatic ductal adenocarcinoma cell lines.NHF-1 (Fibroblast) MiaPaca2, Panc1, CAPAN1 & BxPC3 cells were harvested for RNA & protein following 24 hours exposure to normoxia (21% O2) or hypoxia (1% O2). (A) Phase-contrast images at 10× magnification were taken of MiaPaca2 (mesenchymal-like) morphology & BxPC3 cells (differentiated, epithelial morphology) under normoxic conditions. (B) PHD3 mRNA expression was determined by qRT-PCR & graphed relative to BxPC3 in normoxia. All samples were normalized to 18S rRNA & graphed as expression relative to BxPC3-Vec Normoxia (lane 1). n = 3, error bars = 1 S.D. (C) Whole cell lysate was resolved by SDS-PAGE & blotted for beta -tubulin PHD3 & PHD2. N = normoxia, H = hypoxia (1% O2). Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0083021), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: EGLN1/PHD2 Antibody [NB100-137] - Iron supplementation restores HIF-1 alpha levels to normal following ATP6V0E1 inhibition in HeLa cells. (A) Schematic diagram of the multimeric V-ATPase complex. (B) Chemical inhibition of V-ATPase by 10 nM BafA treatment for 24 h, increased HIF-1 alpha levels in HIF alpha -GFPODD reporter cells. Treatment with 100 μM Fe (III) citrate significantly reduced the elevated HIF-1 alpha levels associated with loss of ATP6V0E1 (1 × 106 cells per sample harvested & analyzed; N = 2). (C) Knock-down of ATP6V0E1 subunit with three different CRISPR-Cas9 guides resulted in significant upregulation of HIF-1 alpha levels in HIF alpha -GFPODD reporter cells. Co-treating cells with 100 μM Fe (III) citrate led to a reduction in HIF-1 alpha levels across the three ATP6V0E1 depleted cells. phd2 was knocked down as a control & treatment with 100 μM Fe (III) citrate did not result in reduction of HIF-1 alpha levels (1 × 106 cells per sample harvested & analyzed; N = 2). FACs plot shown is a representative image of two biological repeats performed. (D) Immunoblot analysis for HIF-1 alpha & PHD2 levels in HIF alpha -GFPODD reporter cells with either ATP6V0E1 or PHD2 depleted or treated with 10 nM BafA. The cells were treated with 100 μM Fe (III) citrate for 24 h. beta actin was used as a control. Results validated findings observed by flow cytometry, whereby HIF-1 alpha levels were upregulated following ATP6V0E1 knock-down or inhibition & levels were re-normalized upon Fe (III) citrate treatment. Treatment of Fe (III) citrate in PHD2 depleted cells did not alter HIF-1 alpha levels. All experiments were performed in biological duplicate. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32984302), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: EGLN1/PHD2 Antibody [NB100-137] - PHD3 depletion stabilizes hypoxic p27 expression by increasing p27 half-life. a Cell cycle arrest at G0 & subsequent release shows an increase of p27 expression in siPHD3 exposed cells. b Quantification for p27 expression under PHD3 depletion at indicated time points after cell cycle release in HeLa & 786-O cells. Asterisk indicates significant difference (p < 0,05; n = 3). c Cell cycle arrest at G0 & inhibition of protein synthesis with cycloheximide indicate increased p27 stability in PHD3 depleted HeLa cells. d Quantification of p27 expression using siPHD3 or control at indicated time points. Four independent experiments (± SEM) are shown (p < 0,05; n = 4). e Analysis of p27 stability in 786–0 cells by cycloheximide chase during reoxygenation after 24 h hypoxia demonstrates markedly increased half-life of p27 upon PHD3 depletion Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26223520), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Pm, Pm-Or, Rb, RM

Species Glossary

Reactivity: Hu, Mu, Rt, Pm, Pm-Or, Rb, RM

Applications:

, , , , , , ,

Applications: , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-137AF350
Alexa Fluor 405	NB100-137AF405
Alexa Fluor 488	NB100-137AF488
Alexa Fluor 532	NB100-137AF532
Alexa Fluor 594	NB100-137AF594
Alexa Fluor 647	NB100-137AF647
Alexa Fluor 700	NB100-137AF700
Alexa Fluor 750	NB100-137AF750
Allophycocyanin	NB100-137APC
Biotin	NB100-137B
CoraFluor 1	NB100-137CL1
DyLight 350	NB100-137UV
DyLight 405	NB100-137V
DyLight 488	NB100-137G
DyLight 550	NB100-137R
DyLight 594	NB100-137DL594
DyLight 650	NB100-137C
DyLight 680	NB100-137FR
DyLight 755	NB100-137IR
FITC	NB100-137F
HRP	NB100-137H
Janelia Fluor 525	NB100-137JF525
Janelia Fluor 549	NB100-137JF549
Janelia Fluor 646	NB100-137JF646
Janelia Fluor 669	NB100-137JF669
PE	NB100-137PE
PerCP	NB100-137PCP
mFluor Violet 450 SE	NB100-137MFV450
mFluor Violet 500 SE	NB100-137MFV500
mFluor Violet 610 SE	NB100-137MFV610

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NB600-502

GAPDH Antibody (6C5cc) - BSA Free

(3 Reviews)

(87 Publications)

0.2 mg

NB600-502

Western Blot: GAPDH Antibody (6C5) [NB600-502] - Western blot of FGF23 in the kidney. GAPDH antibody (6C5) served as an internal control. Each value represents the mean +/- SEM. Citation: Sugiura H, Matsushita A, Futaya M, Teraoka A, Akiyama K-i, Usui N, et al. (2018) Fibroblast growth factor 23 is upregulated in the kidney in a chronic kidney disease rat model. PLoS ONE 13(3): e0191706. //doi.org/10.1371/journal.pone.0191706

Simple Western: GAPDH Antibody (6C5) [NB600-502] - Simple Western lane view shows a specific band for GAPDH in 0.5 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system. Note: band observed higher than predicted 36 kDa molecular weight.

Simple Western: GAPDH Antibody (6C5) [NB600-502] - Anaylsis in rat brain and spinal cord. This image includes the GAPDH at the predicted kDa as well as a glucocorticoid receptor antibody (peak 102). Verified customer review.

Western Blot: GAPDH Antibody (6C5cc) [NB600-502] - Western blot analysis for whole cell & nuclear signal transduction proteins. (A) Phosphorylated FAK (Y397) was significantly decreased at 24 h & significantly increased at 48 h as compared to sham. (B) Nuclear localization of corresponding signal transduction molecules, p38, & p65, were decreased at 24 h & increased at 48 h as compared to sham. *p 0.05.Immortalized Brca1F/C61G MEFs were infected with retroviruses expressing the indicated shRNAs and/or Cre recombinase, followed by selection with puromycin for 72 h. The frequency of end-to-end chromosome-type fusions was analysed as in (A).MEFs of the indicated genotypes were infected with retroviruses expressing TRF2 and/or CtIP shRNAs, followed by selection with puromycin for 72 h. Cell extracts were prepared 48 h later & analysed by Western blotting as indicated. GAPDH was used as a loading control. *non-specific band. Cells treated as in (C) & (E) were arrested in mitosis with colcemid, & mitotic chromosomes isolated 48 h later were fixed & stained with a Cy3-conjugated (CCCTAA)3-PNA probe (D, F). The frequency of end-to-end chromosome-type fusions is represented as a percentage of fusions observed after TRF2 depletion. Error bars represent SD of two independent experiments. P-values were calculated using an unpaired two-tailed t-test. *P ≤ 0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25582120), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Am, Ca, ChHa, Fe, Fi, Rb, Bv(-), Gt(-)

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Am, Ca, ChHa, Fe, Fi, Rb, Bv(-), Gt(-)

Applications:

, , , , ,

Applications: , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB600-502AF350-0.2ml
Alexa Fluor 405	NB600-502AF405-0.2ml
Alexa Fluor 488	NB600-502AF488-0.2ml
Alexa Fluor 532	NB600-502AF532-0.2ml
Alexa Fluor 594	NB600-502AF594-0.2ml
Alexa Fluor 647	NB600-502AF647-0.2ml
Alexa Fluor 700	NB600-502AF700-0.2ml
Alexa Fluor 750	NB600-502AF750-0.2ml
Biotin	NB600-502B-0.2ml
CoraFluor 1	NB600-502CL1
DyLight 350	NB600-502UV-0.2ml
DyLight 405	NB600-502V-0.2ml
DyLight 488	NB600-502G-0.2ml
DyLight 550	NB600-502R-0.2ml
DyLight 594	NB600-502DL594-0.2ml
DyLight 650	NB600-502C-0.2ml
DyLight 680	NB600-502FR-0.2ml
DyLight 755	NB600-502IR-0.2ml
FITC	NB600-502F-0.2ml
HRP	NB600-502H-0.2ml
Janelia Fluor 525	NB600-502JF525
Janelia Fluor 549	NB600-502JF549-0.2ml
Janelia Fluor 646	NB600-502JF646-0.2ml
Janelia Fluor 669	NB600-502JF669
mFluor Violet 450 SE	NB600-502MFV450
mFluor Violet 500 SE	NB600-502MFV500
mFluor Violet 610 SE	NB600-502MFV610

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NB100-56113

Caspase-3 Antibody - (active/cleaved) - BSA Free

(81 Publications)

0.05 ml

NB100-56113

Western Blot: Caspase-3 Antibody - (active/cleaved) [NB100-56113] - Cell apoptosis was detected by flow cytometric analysis, and the percentage of apoptotic cells transfected with miR-200c inhibitor or NC inhibitor and treated with AngII or PBS for 48 h was determined. Image collected and cropped by CiteAb from the following publication (onlinelibrary.wiley.com/doi/abs/10.1111/jcmm.14135), licensed under a CC-BY license.

Immunohistochemistry-Paraffin: Caspase-3 Antibody - (active/cleaved) [NB100-56113] - Dog ischemic brain stained for Active/Cleaved Caspase-3 expression using Caspase-3 Antibody - (active/cleaved)( NB100-56113) at 1:2000. Staining is seen in the nuclei of dying neurons (black arrow) but not in the morphologically normal nuclei (open arrows). Caspase-3 expression in the nucleus is considered to be a marker of active/caspase-3 expression and apoptosis. Hematoxylin-eosin counterstain.

Immunohistochemistry-Paraffin: Caspase-3 Antibody - (active/cleaved) [NB100-56113] - Irradiated mouse spleen stained for Active/Cleaved Caspase-3 expression using Caspase-3 Antibody - (active/cleaved) (NB100-56113) at 1:2000. Staining is seen in the nuclei of a subset of the cell population. Caspase-3 expression in the nucleus is considered to be a marker of active/caspase-3 expression and apoptosis. Hematoxylin-eosin counterstain.

Antidepressants-mediated effect on cellular protein content. HT-22 cells were treated with antidepressants for 48 and 96 h and densitometry analysis of NF-kappa B (b), p16 (c), p21 (d), p27 (e), p53 (f), TRF1 (g), TRF2 (h), calnexin (i), NuMa (j), cleaved caspase 3 (k), Bcl-2 (l) was evaluated. Representative Western Blots are presented (a). Bars indicate SD, n = 3, ***/^^^p < 0.001, **/^^p < 0.01, */^p < 0.05, no indication—no statistical significance (one-way ANOVA and Dunnett’s a posteriori test)

Immunohistochemistry: Caspase-3 Antibody - (active/cleaved) [NB100-56113] - Pathology in DOX treated acute & recovery phase mice. Regions of myofiber loss & frank replacement fibrosis were noted, most commonly in atria (A, acute phase), & rarely in ventricles (D, recovery phase). These areas were accompanied by macrophage infiltration (B, E) & myofibroblast proliferation (C) consistent with fibroplasia. Rare myofibers were matrix metalloproteinase 2 (F, recovery phase animal) or caspase-3 positive (G, acute phase animal). Reticulin staining (A, D); Immunohistochemistry: Iba 1(B, E; macrophages), alpha SMA (C), MMP-2 (F) & cleaved caspase -3 (G) Bar = 100µm (A-C); 50µm (D-F); 20µm (G). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31263061), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: Caspase-3 Antibody - (active/cleaved) [NB100-56113] - Antidepressants-mediated effect on cellular protein content. HT-22 cells were treated with antidepressants for 48 & 96 h & densitometry analysis of NF-kappa B (b), p16 (c), p21 (d), p27 (e), p53 (f), TRF1 (g), TRF2 (h), calnexin (i), NuMa (j), cleaved caspase 3 (k), Bcl-2 (l) was evaluated. Representative Western Blots are presented (a). Bars indicate SD, n = 3, ***/^^^p < 0.001, **/^^p < 0.01, */^p < 0.05, no indication—no statistical significance (one-way ANOVA & Dunnett’s a posteriori test) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31278507), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: Caspase-3 Antibody - (active/cleaved) [NB100-56113] - Morphological changes & expression of key apoptosis-related molecules in 4T1 cells after DE-EDCP treatment(A) Morphological changes of 4T1 cells exposed to various concentrations of DE-EDCP for 24h. (B) Immunofluorescence staining for Bcl-2 (green), Bax (green) & cleaved caspase-3 (green) together with DNA staining with DAPI (blue) in 4T1 cells incubated with DE-EDCP or cisplatin (31.25 μM) for 24h, as well as in untreated cells (magnification at x200). (C) mRNA expression of Bcl-2, Bax & caspase-3 quantified by RT-PCR in 4T1 cells after DE-EDCP 24h treatment. DE-EDCP treatment markedly increased the expression of Bax & caspase-3 mRNA & decreased the expression of Bcl-2 mRNA in 4T1 cells. beta -actin mRNA was used as an internal control. Data points are represented by the expression ratio & mean±SD fold of control in 4T1 cells. (* Bcl-2-: DE-EDCP vs. untreated p=0.03; DE-EDCP vs. cisplatin p=0.006; cislatin vs. untreated p=0.001; Bax-: DE-EDCP vs. untreated p=0.011; cislatin vs. untreated p=0.009; caspase-3-: DE-EDCP vs. untreated p=0.015; DE-EDCP vs. cisplatin p=0.021) Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.25610), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Ma

Species Glossary

Reactivity: Hu, Mu, Rt, Ma

Applications:

, , , , ,

Applications: , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Alt Catalog#

IMG-5700

Alt Catalog# IMG-5700

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Validated by:

Validated by:

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-56113SS

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NB600-582

SREBP1 Antibody (2A4) - BSA Free

(73 Publications)

0.1 ml

NB600-582

Simple Western: SREBP1 Antibody (2A4) [NB600-582] - Lane view shows a specific band for SREBP1 in 1.0 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.

<b>Genetic Strategies Validation. </b>Western Blot: SREBP1 Antibody (2A4) [NB600-582] - KO and OE of SREBP1 influenced lipid metabolism in Bel-7402 cells. The protein level of lipid-associated genes in SREBP1-KO, SREBP1-OE, and WT Bel-7402 cells. Data were expressed as mean -/+ standard error of the mean. *P < 0.05, **P < 0.01, and ***P < 0.001 vs. WT group, respectively.

Western Blot: SREBP1 Antibody (2A4) - BSA Free [NB600-582] - Effect of GEN on the expression of Nrf2‐related signalling proteins in OA (660 μmol/L) & PA (330 μmol/L)‐induced HepG2 cells. GEN was added into HepG2 cells prior 1 h to stimulation of OA & PA for 18 h. A‐C, Protein expression of Nrf2, PPAR alpha , PPAR gamma in nucleus & HO‐1 in cytoplasm was detected by Western blot. (D & E) Protein expression of P‐ACC, ACC, P‐AKT, AKT, P‐AMPK alpha , AMPK alpha , P‐AMPK beta & AMPK beta was detected by Western blot. F‐H, Protein expression of PI3K, P‐mTORC, mTORC, P‐S6K, S6K, P‐S6, S6, SREBP‐1c & HMGB1 was detected by Western blot. The similar results were collected from three dependent experiments. All data were expressed by mean ± SEM (n = 5 in each group). ##P < .01 vs Control Group; *P < .05 & **P < .01 vs OA & PA Group Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32293113), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: SREBP1 Antibody (2A4) - BSA Free [NB600-582] - KO & OE of SREBP1 influenced lipid metabolism in Bel-7402 cells. (A) Total cellular TG content of SREBP1-KO, SREBP1-OE, & WT Bel-7402 cells. (B) HPLC-MS determination of the SFAs to MUFAs ratios (palmitic acid to palmitoleic acid, 16:0 to 16:1) (stearic acid to oleic acid, 18:0 to 18:1) as well as the content of 16:0, 16:1, 18:0, & 18:1 in SREBP1-KO, SREBP1-OE, & WT Bel-7402 cells. (C) The transcript level of lipid-associated genes in SREBP1-KO, SREBP1-OE, & WT Bel-7402 cells. (D & E) The protein level of lipid-associated genes in SREBP1-KO, SREBP1-OE, & WT Bel-7402 cells. Data were expressed as mean ± standard error of the mean. *P < 0.05, **P < 0.01, & ***P < 0.001 vs. WT group, respectively. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31297058), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: SREBP1 Antibody (2A4) - BSA Free [NB600-582] - Construction of knockout (KO) & overexpression (OE) cell lines. (A) The sequencing results of KO positive clone cells; (B) The messenger RNA (mRNA) level of SREBP1 in wild type (WT) & OE Bel-7402 cells. Data were expressed as mean ± standard error of the mean. ***P < 0.001 vs. WT group; (C & D) The protein level of SREBP1 in WT, OE, & KO Bel-7402 cells. Data were expressed as mean ± standard error of the mean. ***P < 0.001 vs. WT group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31297058), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: SREBP1 Antibody (2A4) - BSA Free [NB600-582] - p75NTR stimulation activated SREBP1 & SREBP2 in Huh7 hepatocyte cells.Human Huh7 cells were stimulated with 10 ng/ml pro-NGF or 50 ng/ml NGF for 16 h followed by immunoblotting using antibodies to detect the presence of cleaved/activated SREBP1 & SREBP2. a SREBP1, immunoblots & b quantification. Values are mean ± SD, n = 3. **P < 0.01 & *p < 0.05 for treated vs. control cells. c, d SREBP2. Cells were treated with 10 ng/ml pro-NGF in the absence or presence of 0.5 μM PF429242 (PF), which is a selective inhibitor of the Site 1 protease (S1P). c Immunoblots & d quantification. PF decreased the amount of processed SREBP2 in these cells; however, addition of pro-NGF increased the relative level of cleaved SREBP2. Values are mean ± SD, n = 3. *p < 0.05 for treated vs. the corresponding control Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31296846), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: SREBP1 Antibody (2A4) - BSA Free [NB600-582] - Effect of GEN on the protein expression of Nrf2, ACC & mTORC signalling pathways in tyloxapol‐induced mice. GEN (50, 75, 100 mg/kg) was administered to WT or Nrf2−/− mice prior 1 h to stimulation of tyloxapol (500 mg/kg) for 18 h. A‐C, Protein expression of Nrf2, PPAR alpha , PPAR gamma in nucleus & HO‐1 in cytoplasm of WT mice was detected by Western blot. (D & E) Protein expression of Nrf2, PPAR alpha & PPAR gamma in Nrf2−/− mice was detected by Western blot. F‐H, Protein expression of P‐ACC, ACC, P‐AKT, AKT, P‐AMPK alpha , AMPK alpha , P‐AMPK beta , AMPK beta in WT & Nrf2−/− mice was detected by Western blot. I‐M, Protein expression of PI3K, P‐mTORC, mTORC, P‐S6K, S6K, P‐S6, S6, SREBP‐1c & HMGB1 WT & Nrf2−/− mice was detected by Western blot. The similar results were collected from three dependent experiments. All data were expressed by mean ± SEM (n = 5 in each group). ##P < .01 vs Control group; *P < .05 & **P < .01 vs Tyloxapol group Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32293113), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Ca, Ch, Ha, Pm, SyHa

Species Glossary

Reactivity: Hu, Mu, Rt, Ca, Ch, Ha, Pm, SyHa

Applications:

, , ,

Applications: , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB600-582AF350
Alexa Fluor 405	NB600-582AF405
Alexa Fluor 488	NB600-582AF488
Alexa Fluor 532	NB600-582AF532
Alexa Fluor 594	NB600-582AF594
Alexa Fluor 647	NB600-582AF647
Alexa Fluor 700	NB600-582AF700
Alexa Fluor 750	NB600-582AF750
Allophycocyanin	NB600-582APC
Biotin	NB600-582B
CoraFluor 1	NB600-582CL1
DyLight 350	NB600-582UV
DyLight 405	NB600-582V
DyLight 488	NB600-582G
DyLight 550	NB600-582R
DyLight 594	NB600-582DL594
DyLight 650	NB600-582C
DyLight 680	NB600-582FR
DyLight 755	NB600-582IR
FITC	NB600-582F
HRP	NB600-582H
Janelia Fluor 525	NB600-582JF525
Janelia Fluor 549	NB600-582JF549
Janelia Fluor 646	NB600-582JF646
Janelia Fluor 669	NB600-582JF669
PE	NB600-582PE
PerCP	NB600-582PCP
mFluor Violet 450 SE	NB600-582MFV450
mFluor Violet 500 SE	NB600-582MFV500
mFluor Violet 610 SE	NB600-582MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB600-582SS
Azide and BSA Free	NBP2-80959

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NB300-320

GAPDH Antibody

(2 Reviews)

(69 Publications)

0.1 mg

NB300-320

Immunohistochemistry-Paraffin: GAPDH Antibody [NB300-320] - Staining of paraffin embedded Human Pancreas. Antibody at 2.5 ug/mL. Steamed antigen retrieval with citrate buffer pH 6, AP-staining.

Western Blot: GAPDH Antibody [NB300-320] - stai Mutants Have Reduced Levels of alpha-Tubulin, Acetylated alpha-Tubulin, and Kinesin Heavy Chain Protein. Representative western blots of total protein extracted from stai mutant third instar larvae. Heterozygous stai/+ mutant larvae exhibit mild reductions in the levels of alpha-tubulin and acetylated alpha-tubulin compared with wild type larvae. Homozygous stai mutant larvae have dramatic reductions in the levels of alpha-tubulin, acetylated alpha-tubulin and the heavy chain subunit of the microtubule motor protein kinesin compared to wildtype. Df(2L) BSC239 represents a second chromosomal deficiency that excludes the stai gene. GAPDH is used as a loading control. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0068324), licensed under a CC-BY license.

Western Blot: GAPDH Antibody [NB300-320] - Staining of HEK293 (A) and HeLa (B) cell lysate (35 ug protein in RIPA buffer). Antibody at 0.001 ug/mL. Detected by chemiluminescence. Approx 36 kDa band observed in lysates of cell line HEK293 and approx. 35 kDa in HeLa cell lysates.(calculated MW of 36.1 kDa according to Human NP_002037.2).

Immunocytochemistry/Immunofluorescence: GAPDH Antibody [NB300-320] - Immunofluorescence analysis of paraformaldehyde fixed A549 cells, permeabilized with 0.15% Triton. Primary incubation 1hr (10 ug/mL) followed by Alexa Fluor 488 secondary antibody (2 ug/mL), showing cytoplasmic and vesicle staining. The nuclear stain is DAPI (blue). Negative control: Unimmunized goat IgG (10 ug/mL) followed by Alexa Fluor 488 secondary antibody (2 ug/mL). Strong expression of the protein seen in the cytoplasm and vesicles of A549 cells.

Immunohistochemistry-Paraffin: GAPDH Antibody [NB300-320] - Upregulation of GAPDH and Tom20 in C6 gliomas. A small glioma labeled with antibodies against GAPDH. The brightness and contrast have been increased. Image collected and cropped by CiteAb from the following publication (//www.biomedcentral.com/1756-0500/8/207), licensed under a CC-BY license.

Upregulation of GAPDH & Tom20 in C6 gliomas. a A section of rat brain stained with hematoxilin & eosin to show a glioma produced by implantation of C6 cells in the right caudate nucleus. In this case, cells also grew in the region of the syringe needle track through the cortex. (b–d). A small glioma labeled by bisbenzamide (b) & with antibodies against Tom20 (c) & GAPDH (d). The brightness & contrast have been increased. e Illustration of a strip perpendicular to the rim of a glioma (labeled with bisbenzamide) & along which intensity profiles were measured. f, g Tom20 & GAPDH fluorescence along such a strip (barely visible without enhancement). The graphs show the raw intensity values given by ImageJ. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26032618), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody [NB300-320] - PAR2 causes contraction of smooth muscle cells from human prostate. (A & B) Decrease in diameter of collagen hydrogels after PAR2 activation with SLIGKV (80 µM). (C) Representative western blot & (D) densitometry showing time dependent increase in level of phosphorylated MLC20 in PSMC after PAR2 is activated. Data represent mean ± SEM of at least three independent experiments. Diameter of collagen hydrogels were measured in ImageJ (version 1.50i) & significance analyzed in Prism (version 7.04) with one‐way ANOVA followed by Tukey's multiple comparison test. *P < 0.05, **P < 0.01 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31198907), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: GAPDH Antibody [NB300-320] - Upregulation of GAPDH & Tom20 in C6 gliomas. a A section of rat brain stained with hematoxilin & eosin to show a glioma produced by implantation of C6 cells in the right caudate nucleus. In this case, cells also grew in the region of the syringe needle track through the cortex. (b–d). A small glioma labeled by bisbenzamide (b) & with antibodies against Tom20 (c) & GAPDH (d). The brightness & contrast have been increased. e Illustration of a strip perpendicular to the rim of a glioma (labeled with bisbenzamide) & along which intensity profiles were measured. f, g Tom20 & GAPDH fluorescence along such a strip (barely visible without enhancement). The graphs show the raw intensity values given by ImageJ. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26032618), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody [NB300-320] - CDC20B was the protein effector regulated by hsa-miR-633. (a) CDC20B level was up-regulated after ox-LDL treatment revealed by Western blotting. (b) CDC20B level was decreased after the treatment of hsa-miR-633 mimics revealed by Western blotting. (c) CDC20B level was increased after the treatment of hsa-miR-633 inhibitor revealed by Western blotting. (d) The luciferase reporter plasmids were constructed as illustrated. (e) Relative luciferase activities after co-transfection CDC20B WT & hsa-miR-633/Control, or CDC20B Mut & hsa-miR-633/Control were measured. (f) The expression levels of two proliferation markers, Ki67 & PCNA after the treatment of si-CDC20B were measured using Western blotting. (g) Colony formation assay was conducted to examine the proliferation abilityafter the treatment of si-CDC20B. (h) Transwell migration & invasion assays were conducted to examine the migration & invasion abilities of VSMCs after the treatment of si-CDC20B. (i) Quantification results of (g). (j) Quantification results of (h). *P < 0.05, **P < 0.01, ***P < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35212610), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Simple Western: GAPDH Antibody [NB300-320] - MiR-34a affects stroke outcomes via interacting with cytochrome c. (A) WES system image showing CYC, VDAC & GAPDH expression from hemispheres of WT & miR-34a−/− mice at 6 h post-stroke. (B) Relative CYC expression normalized to GAPDH from the data generated by the WES system. CYC level is significantly decreased in ischemic hemispheres of WT mice but no significant changes in miR-34a−/− mice between contralateral hemispheres (Control) & ischemic hemispheres (Ischemia). N = 5 per group, **p < 0.01, One-way ANOVA followed by post hoc Tuckey’s test was used for data analysis. Data are expressed as mean ± S.D. (C) Relative VDAC expression normalized to GAPDH from the data generated by the WES system. VDAC was not significantly altered in WT mice nor miR-34a−/− mice. (D) Multiplexed WES system image showing CYC & GAPDH expression from purified pCECs of WT & miR-34a−/− mice (n = 10 per group, pooled cell samples) at 6 h post-stroke. (E) Relative CYC expression by normalization to GAPDH. A 2.8 fold decrease of CYC level was observed in WT mice but no changes were observed in miR-34a−/− mice between contralateral hemispheres & ischemic hemispheres. (F) A CYC reporter was coexpressed with a miR-34a plasmid, a miR-34a mimic, a miR-34c mimic, or a plasmid control in cultured cerebral vascular endothelial cells for 24 hours. Relative firefly luciferase activity was evaluated & normalized to renilla luciferase activity. Relative firefly luciferase activity was reduced by miR-34a plasmid & miR-34a mimic. The experiment was repeated 3 times & triplicates were used for each analysis. Data represents the mean ± S.D. *p < 0.05. One-way ANOVA followed by post-hoc Tuckey’s test was used for analysis. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32094435), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody [NB300-320] - Hsa-miR-633 inhibitor could reverse the si-circ_0008896 phenotypes. (a) CCK8 assay was conducted to measure cell viability after up-regulation of hsa-miR-633. (b) The expression levels of two proliferation markers, Ki67 & PCNA after up-regulation of hsa-miR-633 were measured using Western blotting. (c) CCK8 assay was conducted to measure cell viability after the treatment of si-circ0008896, hsa-miR-633 inhibitor & si-circ0008896+ hsa-miR-633 inhibitor. (d) The expression levels of two proliferation markers, Ki67 & PCNA after the treatment of si-circ0008896, hsa-miR-633 inhibitor & si-circ0008896+ hsa-miR-633 inhibitor were measured using Western blotting. (e) Colony formation assay was conducted to examine proliferation ability number of colonies after the treatment of si-circ0008896, hsa-miR-633 inhibitor & si-circ0008896+ hsa-miR-633 inhibitor. (f) Quantification results of (e). (g) Transwell migration & invasion assays were conducted to examine the migration & invasion abilities of VSMCs after the treatment of si-circ0008896, hsa-miR-633 inhibitor & si-circ0008896+ hsa-miR-633 inhibitor. (h) Quantification results of (g). *P < 0.05, **P < 0.01, ***P < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35212610), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody [NB300-320] - Down-regulation of hsa_circ_0008896 inhibited proliferation, migration & invasion in vitro. (a) The expression level of hsa_circ_0008896 after si-circ_0008896 transfection was detected using quantitative PCR. (b) CCK8 assay was conducted to measure cell viability after down-regulation of hsa_circ_0008896. (c) The expression levels of two proliferation markers, Ki67 & PCNA after down-regulation of hsa_circ_0008896 were detected using Western blotting. (d) Colony formation assay was conducted to examine proliferation ability after down-regulation of hsa_circ_0008896. (e) The quantification results of (d). (f) Transwell migration & invasion assays were conducted to examine the migration & invasion abilities of VSMCs after down-regulation of hsa_circ_0008896. (g) The quantification results of (f). *P < 0.05, **P < 0.01, ***P < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35212610), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Ca, Dr, I, Po

Species Glossary

Reactivity: Hu, Mu, Rt, Ca, Dr, I, Po

Applications:

, , , , ,

Applications: , , , , ,

Host:

Goat Polyclonal

Host: Goat Polyclonal

Alt Catalog#

IMG-3073

Alt Catalog# IMG-3073

Conjugate:

Unconjugated

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NB100-56503

Cytochrome c Antibody (7H8.2C12) - BSA Free

(62 Publications)

0.1 mg

NB100-56503

Flow (Intracellular): Cytochrome c Antibody (7H8.2C12) [NB100-56503] - An intracellular stain was performed on HeLa cells with Cytochrome c (7H8.2C12) antibody NB100-56503PE (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to phycoerythrin.

Western Blot: Cytochrome c Antibody (7H8.2C12) [NB100-56503] - Human HeLa lysate probed with Cytochrome C antibody at 0.1 ug/ml.

Western Blot: Cytochrome c Antibody (7H8.2C12) [NB100-56503] - Analysis using the biotin conjugate of NB100-56503. Detection of Cytochrome C in 15 ug of HeLa cell lysate using NB100-55775 at 1:1000. A 15 kDa band is detected.

Flow Cytometry: Cytochrome c Antibody (7H8.2C12) [NB100-56503] - Using the Alexa Fluor 488 direct conjugate, an intracellular stain was performed on HeLa cells with Cytochrome c (7H8.2C12) antibody NB100-56503AF488 (blue) and a matched isotype control NBP2-27231AF488 (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 10 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 488.

Simple Western: Cytochrome c Antibody (7H8.2C12) [NB100-56503] - Lane view shows lysates of human heart tissue, loaded at 0.2 mg/mL. A specific band was detected for Cytochrome c at approximately 23 kDa (as indicated) using 2.5 ug/mL of Mouse Anti-Cytochrome c Monoclonal Antibody (Catalog # NB100-56503). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.

Simple Western: Cytochrome c Antibody (7H8.2C12) [NB100-56503] - Cytochrome C Antibodies (NB100-56503SS), ProteinSimple Western Blot on Jess Instrument; 1 microgram of human brain tissue lysate was tested with the antibodies diluted 20 times. Image from verified customer review.

Effects of resveratrol on the expression of SIRT1, PGC-1 alpha , HIF-1 alpha & apoptosis proteins in vivo. (A) Activation of the SIRT1–PGC-1 alpha –HIF-1 alpha signaling pathway in PC–AKI associated with DN in rabbits. Representative western blot images of proteins in the rabbits with DN treated with saline (Cont), resveratrol alone (Res), iohexol (PC–AKI), & co-treatment with resveratrol & iohexol (Res+PC–AKI). (B–H) Relative densitometry analysis of the ratios of SIRT1–PGC-1 alpha –HIF-1 alpha signaling proteins to beta -actin were expressed as mean ± standard error. *P < 0.05 vs. Cont; #P < 0.05 vs. PC–AKI. Cont, control; Res, resveratrol; PC–AKI, post-contrast acute kidney injury; SIRT1, silent information regulator l; HIF-1 alpha , hypoxia-inducible transcription factor-1 alpha ; DN, diabetic nephropathy; PGC-1 alpha , peroxisome proliferator-activated receptor gamma coactivator-1 alpha. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31402864), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Dr, Rb

Species Glossary

Reactivity: Hu, Mu, Rt, Dr, Rb

Applications:

, , , , ,

Applications: , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Alt Catalog#

IMG-101A

Alt Catalog# IMG-101A

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-56503AF350
Alexa Fluor 405	NB100-56503AF405
Alexa Fluor 488	NB100-56503AF488
Alexa Fluor 532	NB100-56503AF532
Alexa Fluor 594	NB100-56503AF594
Alexa Fluor 647	NB100-56503AF647
Alexa Fluor 700	NB100-56503AF700
Alexa Fluor 750	NB100-56503AF750
Allophycocyanin	NB100-56503APC
Biotin	NB100-56503B
Biotin	NB100-55775
CoraFluor 1	NB100-56503CL1
DyLight 350	NB100-56503UV
DyLight 405	NB100-56503V
DyLight 488	NB100-56503G
DyLight 550	NB100-56503R
DyLight 594	NB100-56503DL594
DyLight 650	NB100-56503C
DyLight 680	NB100-56503FR
DyLight 755	NB100-56503IR
FITC	NB100-56503F
HRP	NB100-56503H
Janelia Fluor 525	NB100-56503JF525
Janelia Fluor 549	NB100-56503JF549
Janelia Fluor 646	NB100-56503JF646
Janelia Fluor 669	NB100-56503JF669
PE	NB100-56503PE
PerCP	NB100-56503PCP
mFluor Violet 450 SE	NB100-56503MFV450
mFluor Violet 500 SE	NB100-56503MFV500
mFluor Violet 610 SE	NB100-56503MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-56503SS
Azide and BSA Free	NBP2-80686

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NB100-2215

SREBP1 Antibody - BSA Free

(3 Reviews)

(59 Publications)

0.1 ml

NB100-2215

Western Blot: SREBP1 Antibody [NB100-2215] - MiR-181a overexpression impairs and miR-181a inhibition improves glucose and lipid homeostasis in HepG2 cellsHepG2 cells were divided into 4 groups as follows: a control group, mimics group (HepG2 cells transfected with 10 nM mimics), NEFA group (treated with 1. 2 mM NEFA), and miR-181a + NEFA group (transfected with 50 nM miR-181a inhibitors and then treated with 1. 2 mM NEFA). It was followed with or without 100 nM insulin. Immunoblot analysis (left) and quantification (right) of SREBP-1c and PPARI+- in HepG2 cells. Image collected and cropped by Citeab from the following publication (Upregulation of miR-181a impairs hepatic glucose and lipid homeostasis. Oncotarget (2017)) licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: SREBP1 Antibody [NB100-2215] - SREBP1 antibody was tested in HeLa cells with DyLight488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red). Nuclear and punctate vesicle staining was observed.

Immunohistochemistry-Paraffin: SREBP1 Antibody [NB100-2215] - nalysis of FFPE tissue section of mouse liver with SREBP1 antibody at 1:200. The antibody generated an expected cytoplasmic-nuclear immunostaining of SREBP1 protein in the hepatocytes.

Western Blot: SREBP1 Antibody [NB100-2215] - Detection of SREBP1. Lane 1: human liver. Lane 2: mouse liver.

Western Blot: SREBP1 Antibody - BSA Free [NB100-2215] - MiR-181a overexpression impairs & miR-181a inhibition improves glucose & lipid homeostasis in HepG2 cellsHepG2 cells were divided into 4 groups as follows: a control group, mimics group (HepG2 cells transfected with 10 nM mimics), NEFA group (treated with 1.2 mM NEFA), & miR-181a + NEFA group (transfected with 50 nM miR-181a inhibitors & then treated with 1.2 mM NEFA). B was followed with or without 100 nM insulin. (A) Immunoblot analysis (top) & quantification (bottom) of SIRT1, PGC-1 alpha & acetylated PGC-1 alpha in HepG2 cells. (B) Immunoblotting analysis (top) & quantification (bottom) of insulin-stimulated phosphorylation of AKT in HepG2 cells. (C) Glucose concentration in medium. (D) The glycogen content in HepG2 cells. (E) The mRNA expression levels of G6Pase & PEPCK. (F) Immunoblot analysis (left) & quantification (right) of SREBP-1c & PPAR alpha in HepG2 cells. (G) TG content in HepG2 cells. *P 25 (n = 24). There was no significant difference. (F) The BMI and H-scores of PPAR alpha , SREBP1, and FAS in each EMC patient are shown in scatter plots. Spearman’s rank correlation coefficient showed a weak inverse correlation between BMI and the PPAR alpha H-score and a moderate or weak correlation between BMI and SREBP1 or FAS. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37305395), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Bv, Ha, Pl, ChHa

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Bv, Ha, Pl, ChHa

Applications:

, , , ,

Applications: , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-2215AF350
Alexa Fluor 405	NB100-2215AF405
Alexa Fluor 488	NB100-2215AF488
Alexa Fluor 532	NB100-2215AF532
Alexa Fluor 594	NB100-2215AF594
Alexa Fluor 647	NB100-2215AF647
Alexa Fluor 700	NB100-2215AF700
Alexa Fluor 750	NB100-2215AF750
Allophycocyanin	NB100-2215APC
Biotin	NB100-2215B
CoraFluor 1	NB100-2215CL1
DyLight 350	NB100-2215UV
DyLight 405	NB100-2215V
DyLight 488	NB100-2215G
DyLight 550	NB100-2215R
DyLight 594	NB100-2215DL594
DyLight 650	NB100-2215C
DyLight 680	NB100-2215FR
DyLight 755	NB100-2215IR
FITC	NB100-2215F
HRP	NB100-2215H
Janelia Fluor 525	NB100-2215JF525
Janelia Fluor 549	NB100-2215JF549
Janelia Fluor 646	NB100-2215JF646
Janelia Fluor 669	NB100-2215JF669
PE	NB100-2215PE
PerCP	NB100-2215PCP
mFluor Violet 450 SE	NB100-2215MFV450
mFluor Violet 500 SE	NB100-2215MFV500
mFluor Violet 610 SE	NB100-2215MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-2215SS

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At	=	A. thaliana	SyHa	=	Golden Syrian Hamster
All	=	All Species	Ha	=	Hamster
An	=	Animal	Hu	=	Human
ArHa	=	Armenian Hamster	I	=	Insect
Av	=	Avian	Ll	=	Llama
Bb	=	Baboon	Ma	=	Mammal
Ba	=	Bacteria	Mk	=	Monkey
Bv	=	Bovine	Mu	=	Mouse
Ca	=	Canine	Multi	=	Multi-species
Ce	=	C. Elegans	NA	=	Non-species specific
Ch	=	Chicken	Or	=	Orangutan
ChHa	=	Chinese Hamster	Pl	=	Plant
Cm	=	Cynomolgus Monkey	Pm	=	Primate
Do	=	Donkey	Po	=	Porcine
Dr	=	Drosophilia	Rb	=	Rabbit
Ec	=	E. Coli	Rt	=	Rat
Eq	=	Equine	RM	=	Rhesus Macaque
Fe	=	Feline	Sh	=	Sheep
Ft	=	Ferret	Vb	=	Vertebrate
Fi	=	Fish	Vi	=	Virus
Fu	=	Fungi	Xp	=	Xenopus
Ge	=	Gerbil	Ye	=	Yeast
GP	=	Guinea Pig	Ze	=	Zebrafish
Gt	=	Goat

Category

Protein/Target

Applications

Reactivity

Citation

Antibody Validation

Reviews

Host

Available Conjugates

Format

Marker

Modification

Clonality

Clone

Gene Symbol

Images Type

Isotype

Kit Type

Lysate Type

Preservative

Protein Or Peptide

Research Areas

Has Sample Size

Promotional Item

Species Glossary

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